Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor

Tracheal cytotoxin (TCT), a naturally occurring fragment of Gram-negative peptidoglycan, is a potent elicitor of innate immune responses in Drosophila. It induces the heterodimerization of its recognition receptors, the peptidoglycan recognition proteins (PGRPs) LCa and LCx, which activates the immune deficiency pathway. The crystal structure at 2.1 angstrom resolution of TCT in complex with the ectodomains of PGRP-LCa and PGRP-LCx shows that TCT is bound to and presented by the LCx ectodomain for recognition by the LCa ectodomain; the latter lacks a canonical peptidoglycan-docking groove conserved in other PGRPs. The interface, revealed in atomic detail, between TCT and the receptor complex highlights the importance of the anhydro-containing disaccharide in bridging the two ectodomains together and the critical role of diaminopimelic acid as the specificity determinant for PGRP interaction.     

A novel nucleoprotein complex at a replication origin

The viral protein p6, required for the protein-primed initiation of replication of Bacillus subtilis phage phi 29, forms a nucleoprotein complex at the viral replication origins that shows novel features. Deoxyribonuclease I and hydroxyl radical footprinting data, as well as the induction of positive supercoiling, support a model in which a DNA right-handed superhelix tightly wraps around a multimeric p6 core. The interaction occurs through the DNA minor groove. The activity of p6 not only requires the formation of the complex but also its correct positioning, indicating that the other proteins involved in the initiation of replication recognize, at a precise position, either the p6 core or the DNA conformational change induced by p6.     

Structural basis of DNA replication origin recognition by an ORC protein

DNA replication in archaea and in eukaryotes share many similarities. We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins. DNA binding is mediated principally by a C-terminal winged helix domain that inserts deeply into the major and minor grooves, widening them both. However, additional DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a characteristic G-rich sequence, inducing a 35 degrees bend in the duplex and providing directionality to the binding site. Both contact regions also induce substantial unwinding of the DNA. The structure provides insight into the initial step in assembly of a replication origin and recruitment of minichromosome maintenance (MCM) helicase to that origin.     

Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

The ubiquitination of the hypoxia-inducible factor (HIF) by the von Hippel-Lindau tumor suppressor (pVHL) plays a central role in the cellular response to changes in oxygen availability. pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1alpha peptide-pVHL-ElonginB-ElonginC complex shows that HIF-1alpha binds to pVHL in an extended beta strand-like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues. Although the beta sheet-like interactions contribute to the stability of the complex, the hydroxyproline contacts are central to the strict specificity characteristic of signaling.     

RNA recognition and cleavage by a splicing endonuclease

The RNA splicing endonuclease cleaves two phosphodiester bonds within folded precursor RNAs during intron removal, producing the functional RNAs required for protein synthesis. Here we describe at a resolution of 2.85 angstroms the structure of a splicing endonuclease from Archaeglobus fulgidus bound with a bulge-helix-bulge RNA containing a noncleaved and a cleaved splice site. The endonuclease dimer cooperatively recognized a flipped-out bulge base and stabilizes sharply bent bulge backbones that are poised for an in-line RNA cleavage reaction. Cooperativity arises because an arginine pair from one catalytic domain sandwiches a nucleobase within the bulge cleaved by the other catalytic domain.     

某大型复杂工程混凝土施工中变形裂缝的控制

从材料与结构的角度分析了某大型客站混凝土结构地下风道施工中出现裂缝的原因并提出解决办法.表明在大型复杂工程的混凝土结构设计和施工中,在按照规范控制变形裂缝的同时,应考虑和注意施工过程中结构构件的受力状态的变化,对混凝土收缩裂缝控制也应涵盖施工全过程.     

复杂环境下香蕉多目标特征快速识别研究

【目的】针对野外环境下断蕾机器人对多特征的变量目标快速识别难题,以及目标受到树叶、遮挡及光照影响精度的问题,提出多特征目标的快速识别方法。【方法】提出对香蕉果实、果轴和花蕾这3个目标进行多尺度特征提取及模型分类,融合聚类算法设计新的目标候选框参数,提出改进YOLOv3模型及网络结构参数的YOLO-Banana模型;为了平衡速度和准确度,用YOLO-Banana和Faster R-CNN分别对变化尺寸的香蕉多目标进行试验,研究算法对识别精度与速度的影响。【结果】YOLO-Banana和Faster R-CNN这2种算法识别香蕉、花蕾和果轴的总平均精度分别为91.03%和95.16%,平均每张图像识别所需时间分别为0.237和0.434 s。2种算法精度均高于90%,YOLO-Banana的速度相对快1.83倍,更符合实时作业的需求。【结论】野外蕉园环境下,采用YOLO-Banana模型进行香蕉多目标识别,可满足断蕾机器人视觉识别的速度及精度要求。     

Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A

The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene expression. The crystal structure of a complex containing the three zinc fingers from Zif268 (a mouse immediate early protein) and a consensus DNA-binding site has been determined at 2.1 angstroms resolution and refined to a crystallographic R factor of 18.2 percent. In this complex, the zinc fingers bind in the major groove of B-DNA and wrap part way around the double helix. Each finger has a similar relation to the DNA and makes its primary contacts in a three-base pair subsite. Residues from the amino-terminal portion of an alpha helix contact the bases, and most of the contracts are made with the guanine-rich strand of the DNA. This structure provides a framework for understanding how zinc fingers recognize DNA and suggests that this motif may provide a useful basis for the design of novel DNA-binding proteins.     

Crystal structure of a complex of acridine, cytosine and water (1:1:1)

X-ray structural analysis of a crystalline complex between acridine C(13)H(9)N, cytosine C(4)H(5)N(3)O, and water (1:1:1) has been completed. The cytosine and water molecules form a sheet-like structure through a series of hydrogen bonds. The acridine molecules are bound to this layer through a hydrogen bridge from the water to the ring nitrogen. The acridine molecules stack in a parallel fashion normal to the cytosine-water sheets, with an average interplanar spacing of 3.5 angstroms.     

Antiviral resistance by the polyinosinic acid-poly (1-vinylcytosine) complex

The antiviral activities of analogs of the double-stranded complex of polyinosinic and polycytidylic acids [poly(I).poly(C)], which is a potent interferon inducer, have been studied. Structural changes that modify the polymer backbone substantially, such as loops or 2' --> 5' phosphodiester bonds, lead to decreased antiviral activity. Unexpectedly, however, the complex of polyinosinic acid and poly(1-vinylcytosine), which is only a much more distantly related analog of poly(I) . poly(C), shows high activity. It is postulated that the high activity is related to the reduction of the charge/mass ratio and to the existence of this complex in an aggregated state; these are two factors that generally enhance the uptake of compo unds by cells.     

Hardening by annealing and softening by deformation in nanostructured metals

We observe that a nanostructured metal can be hardened by annealing and softened when subsequently deformed, which is in contrast to the typical behavior of a metal. Microstructural investigation points to an effect of the structural scale on fundamental mechanisms of dislocation-dislocation and dislocation-interface reactions, such that heat treatment reduces the generation and interaction of dislocations, leading to an increase in strength and a reduction in ductility. A subsequent deformation step may restore the dislocation structure and facilitate the yielding process when the metal is stressed. As a consequence, the strength decreases and the ductility increases. These observations suggest that for materials such as the nanostructured aluminum studied here, deformation should be used as an optimizing procedure instead of annealing.     

基于Mask-RCNN的复杂背景下多目标叶片的分割和识别

在基于叶片图像进行植物识别和生长状态监控时,植物目标叶片的准确分割和识别是前提和基础,但复杂背景给叶片的分割和识别带来了极大的挑战。本研究提出基于Mask-RCNN深度学习网络分割和识别复杂背景下多目标叶片的算法,共拍摄自然生长状态下常见的植物叶片图像7 357张,标注3 000张作为训练数据库,这3 000张图像共包含4种植物,分别为孔雀竹芋(Calathea makoyana)、珊瑚树(Viburnum odoratissinum)、洋常春藤(Hedera helix L.)和黄花羊蹄甲(Bauhinia tomentosa)。选择这4种植物的80个测试样本图像进行分割、识别与错分率分析。结果表明:Mask-RCNN深度学习网络对这4种植物的识别效果良好,未出现误识别的情况;分割的平均图像错分率为0.93%,最大值不超过2.49%,即分割准确率达97.51%;同时该算法具有强大的迁移能力。     

Arthritis provoked by linked T and B cell recognition of a glycolytic enzyme

The hallmark of rheumatoid arthritis (RA) is specific destruction of the synovial joints. In a mouse line that spontaneously develops a disorder with many of the features of human RA, disease is initiated by T cell recognition of a ubiquitously expressed self-antigen; once initiated, pathology is driven almost entirely by immunoglobulins. In this study, the target of both the initiating T cells and pathogenic immunoglobulins was identified as glucose-6-phosphate isomerase, a glycolytic enzyme. Thus, some forms of RA or related arthritides may develop by a mechanism fundamentally different from the currently popular paradigm of a joint-specific T cell response.     

Kinetic scaffolding mediated by a phospholipase C-beta and Gq signaling complex

Transmembrane signals initiated by a broad range of extracellular stimuli converge on nodes that regulate phospholipase C (PLC)-dependent inositol lipid hydrolysis for signal propagation. We describe how heterotrimeric guanine nucleotide-binding proteins (G proteins) activate PLC-βs and in turn are deactivated by these downstream effectors. The 2.7-angstrom structure of PLC-β3 bound to activated Gα(q) reveals a conserved module found within PLC-βs and other effectors optimized for rapid engagement of activated G proteins. The active site of PLC-β3 in the complex is occluded by an intramolecular plug that is likely removed upon G protein-dependent anchoring and orientation of the lipase at membrane surfaces. A second domain of PLC-β3 subsequently accelerates guanosine triphosphate hydrolysis by Gα(q), causing the complex to dissociate and terminate signal propagation. Mutations within this domain dramatically delay signal termination in vitro and in vivo. Consequently, this work suggests a dynamic catch-and-release mechanism used to sharpen spatiotemporal signals mediated by diverse sensory inputs.     

Acetylcholine binding by a synthetic receptor: implications for biological recognition

The neurotransmitter acetylcholine (ACh) is bound with 50-micromolar affinity by a completely synthetic receptor (host) comprising primarily aromatic rings. The host provided an overall hydrophobic binding site, but one that could recognize the positive charge of the quaternary ammonium group of ACh through a stabilizing interaction with the electron-rich pi systems of the aromatic rings (cation-pi interaction). Similar interactions may be involved in biological recognition of ACh and other choline derivatives.     

Innate recognition of coral snake pattern by a possible avian predator

Inexperienced hand-reared motmots avoided a pattern of red and yellow rings but readily attacked a pattern of green and blue rings and also one of red and yellow stripes. The motmots' avoidance of the "coral snake%" pattern indicates that mimic snake species can derive protection from some potential predators.