典型文献
Crystal structure and catalytic mechanism of the MbnBC holoenzyme required for methanobactin biosynthesis
文献摘要：
Methanobactins(Mbns)are a family of copper-binding peptides involved in copper uptake by methanotrophs,and are potential therapeutic agents for treating diseases characterized by disordered copper accumulation.Mbns are produced via modification of MbnA precursor peptides at cysteine residues catalyzed by the core biosynthetic machinery containing MbnB,an iron-dependent enzyme,and MbnC.However,mechanistic details underlying the catalysis of the MbnBC holoenzyme remain unclear.Here,we present crystal structures of MbnABC complexes from two distinct species,revealing that the leader peptide of the substrate MbnA binds MbnC for recruitment of the MbnBC holoenzyme,while the core peptide of MbnA resides in the catalytic cavity created by the MbnB-MbnC interaction which harbors a unique tri-iron cluster.Ligation of the substrate sulfhydryl group to the tri-iron center achieves a dioxygen-dependent reaction for oxazolone-thioamide installation.Structural analysis of the MbnABC complexes together with functional investigation of MbnB variants identified a conserved catalytic aspartate residue as a general base required for MbnBC-mediated MbnA modification.Together,our study reveals the similar architecture and function of MbnBC complexes from different species,demonstrating an evolutionarily conserved catalytic mechanism of the MbnBC holoenzymes.
文献关键词：
中图分类号：
作者姓名：
Chao Dou;Zhaolin Long;Shoujie Li;Dan Zhou;Ying Jin;Li Zhang;Xuan Zhang;Yanhui Zheng;Lin Li;Xiaofeng Zhu;Zheng Liu;Siyu He;Weizhu Yan;Lulu Yang;Jie Xiong;Xianghui Fu;Shiqian Qi;Haiyan Ren;She Chen;Lunzhi Dai;Binju Wang;Wei Cheng
作者机构：
Division of Respiratory and Critical Care Medicine,Respiratory Infection and Intervention Laboratory of Frontiers Science Center for Disease-related Molecular Network,State Key Laboratory of Biotherapy,West China Hospital of Sichuan University,Chengdu,Sichuan,China;State Key Laboratory of Structural Chemistry of Solid Surface and Fujian Provincial Key Laboratory of Theoretical and Computational Chemistry,College of Chemistry and Chemical Engineering,Xiamen University,Xiamen,Fujian,China;National Institute of Biological Sciences,NIBS,Beijing,China;College of Life Science,Sichuan University,Chengdu,Sichuan,China;Beijing National Laboratory for Molecular Sciences(BNLMS),Beijing Key Laboratory for Magnetoelectric Materials and Devices,College of Chemistry and Molecular Engineering,Peking University,Beijing,China
文献出处：
引用格式：
[1]Chao Dou;Zhaolin Long;Shoujie Li;Dan Zhou;Ying Jin;Li Zhang;Xuan Zhang;Yanhui Zheng;Lin Li;Xiaofeng Zhu;Zheng Liu;Siyu He;Weizhu Yan;Lulu Yang;Jie Xiong;Xianghui Fu;Shiqian Qi;Haiyan Ren;She Chen;Lunzhi Dai;Binju Wang;Wei Cheng-.Crystal structure and catalytic mechanism of the MbnBC holoenzyme required for methanobactin biosynthesis)[J].细胞研究（英文版）,2022(03):302-314
A类：
MbnBC,holoenzyme,Methanobactins,Mbns,MbnA,MbnB,MbnC,MbnABC,oxazolone,thioamide,holoenzymes
B类：
Crystal,catalytic,mechanism,required,methanobactin,biosynthesis,are,family,copper,binding,peptides,involved,uptake,by,methanotrophs,potential,therapeutic,agents,treating,diseases,characterized,disordered,accumulation,produced,via,modification,precursor,cysteine,residues,catalyzed,core,biosynthetic,machinery,containing,iron,dependent,However,mechanistic,details,underlying,catalysis,remain,unclear,Here,present,crystal,structures,complexes,from,two,distinct,species,revealing,that,leader,substrate,binds,recruitment,while,resides,cavity,created,interaction,which,harbors,unique,tri,cluster,Ligation,sulfhydryl,group,center,achieves,dioxygen,reaction,installation,Structural,analysis,together,functional,investigation,variants,identified,conserved,aspartate,general,base,mediated,Together,our,study,reveals,similar,architecture,different,demonstrating,evolutionarily
AB值：
0.489188
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