2011年2月
Crystal structure of bacterial cell-surface alginate-binding protein with an M75 peptidase motif
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- ,
- ,
- ,
- ,
- 巻
- 405
- 号
- 3
- 開始ページ
- 411
- 終了ページ
- 416
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2011.01.043
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
A gram-negative Sphingomonas sp. A1 directly incorporates alginate polysaccharide into the cytoplasm via the cell-surface pit and ABC transporter. A cell-surface alginate-binding protein, Algp7, functions as a concentrator of the polysaccharide in the pit. Based on the primary structure and genetic organization in the bacterial genome, Algp7 was found to be homologous to an M75 peptidase motif-containing EfeO, a component of a ferrous ion transporter. Despite the presence of an M75 peptidase motif with high similarity, the Algp7 protein purified from recombinant Escherichia coli cells was inert on insulin B chain and N-benzoyl-Phe-Val-Arg-p-nitroanilide, both of which are substrates for a typical M75 peptidase. imelysin, from Pseudomonas aeruginosa. The X-ray crystallographic structure of Algp7 was determined at 2.10 angstrom resolution by single-wavelength anomalous diffraction. Although a metal-binding motif, HxxE, conserved in zinc ion-dependent M75 peptidases is also found in Algp7, the crystal structure of Algp7 contains no metal even at the motif. The protein consists of two structurally similar up-and-down helical bundles as the basic scaffold. A deep cleft between the bundles is sufficiently large to accommodate macromolecules such as alginate polysaccharide. This is the first structural report on a bacterial cell-surface alginate-binding protein with an M75 peptidase motif. (C) 2011 Elsevier Inc. All rights reserved.
- リンク情報
-
- DOI
- https://doi.org/10.1016/j.bbrc.2011.01.043
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201102229565975720
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/21238429
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000287996500015&DestApp=WOS_CPL
- ID情報
-
- DOI : 10.1016/j.bbrc.2011.01.043
- ISSN : 0006-291X
- J-Global ID : 201102229565975720
- PubMed ID : 21238429
- Web of Science ID : WOS:000287996500015