Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli
文献类型：期刊论文
| 作者 | Zheng, XM; Hong, J; Li, HY; Lin, DH; Hu, HY |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2012 |
| 卷号 | 1824期号:12页码:1394-1400 |
| 关键词 | CcmH protein topology solution structure redox potential cytochrome c maturation periplasm |
| 通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China.,hyhu@sibs.ac.cn |
| 英文摘要 | In the Gram-negative bacterium of Escherichia coli, eight genes organized as a ccm operon (ccmABCDEFGH) are involved in the maturation of c-type cytochromes. The proteins encoded by the last three genes ccmFGH are believed to form a lyase complex functioning in the reduction of apocytochrome c and haem attachment. Among them, CcmH is a membrane-associated protein; its N-terminus is a catalytic domain with the active CXXC motif and the C-terminus is predicted as a TPR-like domain with unknown function. By using SCAM (scanning cysteine accessibility mutagenesis) and Gaussia luciferase fusion assays, we provide experimental evidence for the entire topological structure of E. coli CcmH. The mature CcmH is a periplasm-resident oxidoreductase anchored to the inner membrane by two transmembrane segments. Both N- and C-terminal domains are located and function in the periplasmic compartment. Moreover, the N-terminal domain forms a monomer in solution, while the C-terminal domain is a compact fold with helical structures. The NMR solution structure of the catalytic domain in reduced form exhibits mainly a three-helix bundle, providing further information for the redox mechanism. The redox potential suggests that CcmH exhibits a strong reductase that may function in the last step of reduction of apocytochrome c for haem attachment. (C) 2012 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | CYTOCHROME-C MATURATION ; COMPLEX-FORMATION ; REDOX PROPERTIES ; APOCYTOCHROME-C ; HEME ; RESTRAINTS ; PATHWAY ; BIOGENESIS ; PERIPLASM ; REDUCTASE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000310761700010 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/667]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Zheng, XM,Hong, J,Li, HY,et al. Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2012,1824(12):1394-1400. |
| APA | Zheng, XM,Hong, J,Li, HY,Lin, DH,&Hu, HY.(2012).Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1824(12),1394-1400. |
| MLA | Zheng, XM,et al."Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1824.12(2012):1394-1400. |
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