3EIW

Crystal structure of Staphylococcus aureus lipoprotein, HtsA

3EIW の概要

• エントリーDOI: 10.2210/pdb3eiw/pdb
• 関連するPDBエントリー: 3eix
• 分子名称: HtsA protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: siderophore, lipoprotein, heme, haem, transport protein
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33394.84

構造登録者

Grigg, J.C.,Murphy, M.E.P. (登録日: 2008-09-17, 公開日: 2009-05-26, 最終更新日: 2024-02-21)

主引用文献

Beasley, F.C.,Vines, E.D.,Grigg, J.C.,Zheng, Q.,Liu, S.,Lajoie, G.A.,Murphy, M.E.,Heinrichs, D.E.
Characterization of staphyloferrin A biosynthetic and transport mutants in Staphylococcus aureus.
Mol.Microbiol., 72:947-963, 2009

PubMed Abstract: Iron is critical for virtually all forms of life. The production of high-affinity iron chelators, siderophores, and the subsequent uptake of iron-siderophore complexes are a common strategy employed by microorganisms to acquire iron. Staphylococcus aureus produces siderophores but genetic information underlying their synthesis and transport is limited. Previous work implicated the sbn operon in siderophore synthesis and the sirABC operon in uptake. Here we characterize a second siderophore biosynthetic locus in S. aureus; the locus consists of four genes (in strain Newman these open reading frames are designated NWMN_2079-2082) which, together, are responsible for the synthesis and export of staphyloferrin A, a polycarboxylate siderophore. While deletion of the NWMN_2079-2082 locus did not affect iron-restricted growth of S. aureus, strains bearing combined sbn and NWMN_2079-2082 locus deletions produced no detectable siderophore and demonstrated severely attenuated iron-restricted growth. Adjacent to NWMN_2079-2082 resides the htsABC operon, encoding an ABC transporter previously implicated in haem acquisition. We provide evidence here that HtsABC, along with the FhuC ATPase, is required for the uptake of staphyloferrin A. The crystal structure of apo-HtsA was determined and identified a large positively charged region in the substrate-binding pocket, in agreement with a role in binding of anionic staphyloferrin A.

PubMed: 19400778
DOI: 10.1111/j.1365-2958.2009.06698.x

実験手法

X-RAY DIFFRACTION (1.6 Å)