标题:Crystal structure of PvdO from Pseudomonas aeruginosa
作者:Yuan, Zenglin; Gao, Fei; Bai, Guohui; Xia, Hengchuan; Gu, Lichuan; Xu, Sujuan
作者机构:[Yuan, Zenglin; Gao, Fei; Bai, Guohui; Gu, Lichuan; Xu, Sujuan] Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Peoples R China.; [Xia 更多
通讯作者:Xu, SJ
通讯作者地址:[Xu, SJ]Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Peoples R China.
来源:BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
出版年:2017
卷:484
期:1
页码:195-201
DOI:10.1016/j.bbrc.2016.12.181
关键词:Pseudomonas aeruginosa; Crystal structure; PvdO; FGE
摘要:Pyoverdine I (PVDI) is a water-soluble fluorescein siderophore with strong iron chelating ability from the gram-negative pathogen Pseudomonas aeruginosa PAO1. Compared to common siderophores, PVDI is a relatively large compound whose synthesis requires a group of enzymes with different catalytic activities. In addition to four nonribosomal peptide synthetases (NRPS) which are responsible for the production of the peptide backbone of PVDI, several additional enzymes are associated with the modification of the side chains. PvdO is one of these enzymes and participates in PVDI precursor maturation in the periplasm. We determined the crystal structure of PvdO at 1.24 angstrom resolution. The PvdO structure shares a common fold with some FGIy-generating enzymes (FGE) and is stabilized by Ca2+. However, the catalytic residues in FGE are not observed in PvdO, indicating PvdO adopts a unique catalytic mechanism. (C) 2017 Elsevier Inc. All rights reserved.
收录类别:SCOPUS;SCIE
WOS核心被引频次:2
Scopus被引频次:2
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85011002380&doi=10.1016%2fj.bbrc.2016.12.181&partnerID=40&md5=f71ee300e1e2e7c8ea3cc21dd153b447
TOP