Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 ? resolution

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• 作者：Xiuhua Liu^a ; ^b ; Qian Du^a ; Zhi Wang^a ; Shiheng Liu^a ; Ning Li^a ; Ying Chen^a ; Chunyuan Zhu^a ; ^c ; Deyu Zhu^a ; Tiandi Wei^a ; Yan Huang^a ; Sujuan Xu^a ; Lichuan Gu^a ; ^{lcgu@sdu.edu.cn}
• 关键词：IPTG ; isopropyl ¦Â-d-1-thiogalactopyranoside ; PMSF ; phenyl methane sulfonyl fluoride ; r.m.s. deviation ; root mean square deviation ; PBP ; periplasmic binding protein ; ABC-transporter ; ATP-binding cassette transporter
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：24 April, 2012
• 年：2012
• 卷：586
• 期：8
• 页码：1240-1244
• 全文大小：1119 K

文摘

VctP, one of the two essential siderophore-binding PBPs from the pathogen Vibrio cholerae, plays an important role in the transport of enterobactin and vibriobactin, which have quite different configurations of iron coordination, from the periplasm to the inner membrane. The current study reports the crystal structure of VctP from V. cholerae N16961 at 1.7 ? resolution. A structural comparison of VctP with its homologues and the results of molecular docking indicate that enterobactin and vibriobactin share the same binding pocket. Significantly, a basic triad consisting of Arg137, Arg226 and Arg270 is used to balance the three negative charges of ferric-enterobactin, while a basic dyad consisting of Arg137 and Arg270 is used to balance the two negative charges of ferric-vibriobactin.