Crystal structure of E. coli ZinT with one zinc-binding mode and complexed with citrate
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chen, Jinli | - |
dc.contributor.author | Wang, Lulu | - |
dc.contributor.author | Shang, Fei | - |
dc.contributor.author | Dong, Yuesheng | - |
dc.contributor.author | Ha, Nam-Chul | - |
dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Quan, Chunshan | - |
dc.contributor.author | Xu, Yongbin | - |
dc.date.accessioned | 2021-09-02T10:21:57Z | - |
dc.date.available | 2021-09-02T10:21:57Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2018-06-02 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/74967 | - |
dc.description.abstract | The ZnuABC ATP-binding cassette transporter found in gram-negative bacteria has been implicated in ensuring adequate zinc import into Zn(II)-poor environments. ZinT is an essential component of ZnuABC and contributes to metal transport by transferring metals to ZnuA, which delivers them to ZnuB in periplasmic zinc recruitment. Although several structures of E. coli ZinT have been reported, its zinc binding sites and oligomeric state have not been clearly identified. Here, we report the crystal structure of E. coli ZinT at 1.76 A resolution. This structure contains one zinc ion in its calycin-like domain, and this ion is coordinated by three highly conserved histidine residues (His167, His176 and His178). Moreover, three oxygen atoms (01, 06 and 07) from the citrate molecule interact with zinc, giving the zinc ion stable octahedral coordination. Our EcZinT structure shows the fewest zinc ions bound of all reported EcZinT structures. Crystallographic packing and size exclusion chromatography suggest that EcZinT prefers to form monomers in solution. Our results provide insights into the molecular function of ZinT. (C) 2018 Published by Elsevier Inc. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | METAL-BINDING | - |
dc.subject | PROTEIN | - |
dc.subject | AFFINITY | - |
dc.subject | CADMIUM | - |
dc.subject | MERCURY | - |
dc.subject | SYSTEM | - |
dc.subject | PHENIX | - |
dc.subject | ROLES | - |
dc.subject | YODA | - |
dc.title | Crystal structure of E. coli ZinT with one zinc-binding mode and complexed with citrate | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Nam, Ki Hyun | - |
dc.identifier.doi | 10.1016/j.bbrc.2018.03.192 | - |
dc.identifier.scopusid | 2-s2.0-85045301385 | - |
dc.identifier.wosid | 000431836700006 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.500, no.2, pp.139 - 144 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 500 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 139 | - |
dc.citation.endPage | 144 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | METAL-BINDING | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | AFFINITY | - |
dc.subject.keywordPlus | CADMIUM | - |
dc.subject.keywordPlus | MERCURY | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | PHENIX | - |
dc.subject.keywordPlus | ROLES | - |
dc.subject.keywordPlus | YODA | - |
dc.subject.keywordAuthor | ZinT | - |
dc.subject.keywordAuthor | Zinc | - |
dc.subject.keywordAuthor | Metal binding | - |
dc.subject.keywordAuthor | Citrate | - |
dc.subject.keywordAuthor | Escherichia coli | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.