Crystal structure of a substrate-binding protein from Rhodothermus marinus reveals a single alpha/beta-domain
- Authors
- Bae, Ji-Eun; Kim, In Jung; Kim, Kyung-Jin; Nam, Ki Hyun
- Issue Date
- 26-2월-2018
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Substrate-binding protein; SBP; ABC transport; alpha/beta-domain
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.497, no.1, pp.368 - 373
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 497
- Number
- 1
- Start Page
- 368
- End Page
- 373
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/77309
- DOI
- 10.1016/j.bbrc.2018.02.086
- ISSN
- 0006-291X
- Abstract
- Substrate-binding proteins (SBPs) bind to specific ligands and are associated with membrane protein complexes for transport or signal transduction. Most SBPs recognize substrates by the hinge motion between two distinct alpha/beta domains. However, short SBP motifs are often observed in protein databases, which are located around methyl-accepting chemotaxis protein genes, but structural and functional studies have yet to be performed. Here, we report the crystal structure of an unusually small SBP from Rhodothermus marinus (named as RmSBP) at 1.9 angstrom. This protein is composed of a single alpha/beta-domain, unlike general SBPs that have two distinct domains. RmSBP exhibits a high structural similarity to the C-terminal domain of the previously reported amino acid bound SBPs, while it does not contain an N-terminal domain for substrate recognition. As a result of the structural comparison analysis, RmSBP has a putative SBP that is different from the previously reported SBP. Our results provide insight into a new class of substrate recognition mechanism by the mini SBP protein. (C) 2018 Elsevier Inc. All rights reserved.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - ETC > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.