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Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM | |
Zhao, Shun1; Wang, Xiao1; Niu, Guoqi2; Dong, Wei1; Wang, Jia1; Fang, Ying1; Lin, Yajing3; Liu, Lin | |
2016 | |
发表期刊 | ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY |
ISSN | 2059-7983 |
卷号 | 72页码:997-1005 |
摘要 | Copper homeostasis integrates multiple processes from sensing to storage and efflux out of the cell. CopM is a cyanobacterial metallochaperone, the gene for which is located upstream of a two-component system for copper resistance, but the molecular basis for copper recognition by this four-helical bundle protein is unknown. Here, crystal structures of CopM in apo, copper-bound and silver-bound forms are reported. Monovalent copper/silver ions are buried within the bundle core; divalent copper ions are found on the surface of the bundle. The monovalent copper/silver-binding site is constituted by two consecutive histidines and is conserved in a previously functionally unknown protein family. The structural analyses show two conformational states and suggest that flexibility in the first alpha-helix is related to the metallochaperone function. These results also reveal functional diversity from a protein family with a simple fourhelical fold. |
关键词 | copper homeostasis copper-binding protein metal coordination helical bundle |
学科领域 | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography |
DOI | 10.1107/S2059798316011943 |
收录类别 | SCI |
语种 | 英语 |
WOS关键词 | SP PCC 6803 ; COPPER RESISTANCE ; CYANOBACTERIAL METALLOCHAPERONE ; MACROMOLECULAR CRYSTALLOGRAPHY ; 2-COMPONENT PROTEINS ; STRUCTURE REFINEMENT ; CENTRAL METABOLISM ; GENE-CLUSTER ; METAL ; HOMEOSTASIS |
WOS研究方向 | Science Citation Index Expanded (SCI-EXPANDED) |
WOS记录号 | WOS:000383998200002 |
出版者 | INT UNION CRYSTALLOGRAPHY |
文献子类 | Article |
出版地 | CHESTER |
资助机构 | National Basic Research Program of ChinaNational Basic Research Program of China [2011CBA00901] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31170688] ; Chinese Academy of SciencesChinese Academy of Sciences [KGZD-EW-T05] |
作者邮箱 | liulin@ibcas.ac.cn |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.ibcas.ac.cn/handle/2S10CLM1/25300 |
专题 | 中科院光生物学重点实验室 |
作者单位 | 1.Chinese Acad Sci, Inst Bot, CAS Ctr Excellence Mol Plant Sci, Key Lab Photobiol, Beijing 100093, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Capital Normal Univ, Coll Life Sci, Beijing 100048, Peoples R China 4.Chinese Acad Sci, Inst Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China |
推荐引用方式 GB/T 7714 | Zhao, Shun,Wang, Xiao,Niu, Guoqi,et al. Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM[J]. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,2016,72:997-1005. |
APA | Zhao, Shun.,Wang, Xiao.,Niu, Guoqi.,Dong, Wei.,Wang, Jia.,...&Liu, Lin.(2016).Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM.ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY,72,997-1005. |
MLA | Zhao, Shun,et al."Structural basis for copper/silver binding by the Synechocystis metallochaperone CopM".ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 72(2016):997-1005. |
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