文献类型：期刊文献

英文题名：Cross-strand disulfides in the hydrogen bonding site of antiparallel beta-sheet (aCSDhs): Forbidden disulfides that are highly strained, easily broken

作者：Haworth, Naomi L.[1,2];Wouters, Michael J.[3];Hunter, Morgan O.[4,5];Ma, Lixia[6];Wouters, Merridee A.[4,5,7]

第一作者：Haworth, Naomi L.

通讯作者：Ma, LX[1];Haworth, NL[2];Wouters, MA[3]

机构：[1]Deakin Univ, Life & Environm Sci, Geelong, Vic, Australia;[2]Victor Chang Cardiac Res Inst, Struct & Computat Biol Div, Sydney, NSW, Australia;[3]Natl Measurement Inst, Elect Sect, Lindfield, NSW, Australia;[4]Olivia Newton John Canc Res Inst, Bioinformat, Heidelberg, Vic, Australia;[5]La Trobe Univ, Sch Canc Med, Melbourne, Vic, Australia;[6]Henan Univ Econ & Law, Sch Stat, Zhengzhou 450046, Henan, Peoples R China;[7]Childrens Med Res Inst, Canc Data Sci, Westmead, NSW, Australia

第一机构：Deakin Univ, Life & Environm Sci, Geelong, Vic, Australia

通讯机构：[1]corresponding author), Henan Univ Econ & Law, Sch Stat, Zhengzhou 450046, Henan, Peoples R China;[2]corresponding author), Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia;[3]corresponding author), Childrens Med Res Inst, Res Inst, Westmead, NSW 2145, Australia.|[1048415]河南财经政法大学统计与大数据学院;[10484]河南财经政法大学;

年份：2019

卷号：28

期号：1

起止页码：239-256

外文期刊名：PROTEIN SCIENCE

收录：;Scopus(收录号：2-s2.0-85058532194);WOS:【SCI-EXPANDED(收录号:WOS:000453579200020)】；

语种：英文

外文关键词：disulfide; redox-active disulfide; thiol-based redox signaling; forbidden; disulfide

摘要：Some disulfide bonds perform important structural roles in proteins, but another group has functional roles via redox reactions. Forbidden disulfides are stressed disulfides found in recognizable protein contexts, which currently constitute more than 10% of all disulfides in the PDB. They likely have functional redox roles and constitute a major subset of all redox-active disulfides. The torsional strain of forbidden disulfides is typically higher than for structural disulfides, but not so high as to render them immediately susceptible to reduction under physionormal conditions. Previously we characterized the most abundant forbidden disulfide in the Protein Data Bank, the aCSDn: a canonical motif in which disulfide-bonded cysteine residues are positioned directly opposite each other on adjacent anti-parallel beta-strands such that the backbone hydrogen-bonded moieties are directed away from each other. Here we perform a similar analysis for the aCSDh, a less common motif in which the opposed cysteine residues are backbone hydrogen bonded. Oxidation of two Cys in this context places significant strain on the protein system, with the beta-chains tilting toward each other to allow disulfide formation. Only left-handed aCSDh conformations are compatible with the inherent right-handed twist of beta-sheets. aCSDhs tend to be more highly strained than aCSDns, particularly when both hydrogen bonds are formed. We discuss characterized roles of aCSDh motifs in proteins of the dataset, which include catalytic disulfides in ribonucleotide reductase and ahpC peroxidase as well as a redox-active disulfide in P1 lysozyme, involved in a major conformation change. The dataset also includes many binding proteins.