1UV7
periplasmic domain of EpsM from Vibrio cholerae
1UV7 の概要
| エントリーDOI | 10.2210/pdb1uv7/pdb |
| 分子名称 | GENERAL SECRETION PATHWAY PROTEIN M (2 entities in total) |
| 機能のキーワード | general secretion pathway, vibrio cholerae, transport |
| 由来する生物種 | VIBRIO CHOLERAE |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 25279.60 |
| 構造登録者 | |
| 主引用文献 | Abendroth, J.,Rice, A.,Mcluskey, K.,Bagdasarian, M.,Hol, W.G.J. The Crystal Structure of the Periplasmic Domain of the Type II Secretion System Protein Epsm from Vibrio Cholerae: The Simplest Version of the Ferredoxin Fold J.Mol.Biol., 338:585-, 2004 Cited by PubMed Abstract: The terminal branch of the general secretion pathway (Gsp or type II secretion system) is used by several pathogenic bacteria for the secretion of their virulence factors across the outer membrane. In these secretion systems, a complex of 12-15 Gsp proteins spans from the pore in the outer membrane via several associated signal or energy-transducing proteins in the inner membrane to a regulating ATPase in the cytosol. The human pathogen Vibrio cholerae uses such a system, called the Eps system, for the export of the cholera toxin and other virulence factors from its periplasm into the lumen of the gastrointestinal tract of the host. Here, we report the atomic structure of the periplasmic domain of the EpsM protein from V.cholerae, which is a part of the interface between the regulating part and the rest of the Eps system. The crystal structure was determined by Se-Met MAD phasing and the model was refined to 1.7A resolution. The monomer consists of two alphabetabeta-subdomains forming a sandwich of two alpha-helices and a four-stranded antiparallel beta-sheet. In the dimer, a deep cleft with a polar rim and a hydrophobic bottom made by conserved residues is located between the monomers. This cleft contains an extra electron density suggesting that this region might serve as a binding site of an unknown ligand or part of a protein partner. Unexpectedly, the fold of the periplasmic domain of EpsM is an undescribed circular permutation of the ferredoxin fold. PubMed: 15081815DOI: 10.1016/J.JMB.2004.01.064 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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