4JER

1.1A resolution Apo structure of the hemophore HasA from Yersinia pestis (Tetragonal Form)

4JER の概要

• エントリーDOI: 10.2210/pdb4jer/pdb
• 関連するPDBエントリー: 4JES 4JET
• 分子名称: Hemophore HasA, SODIUM ION (3 entities in total)
• 機能のキーワード: heme binding protein, transport protein
• 由来する生物種: Yersinia pestis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21048.08

構造登録者

Kumar, R.,Lovell, S.,Battaile, K.P.,Rivera, M. (登録日: 2013-02-27, 公開日: 2013-04-24, 最終更新日: 2023-09-20)

主引用文献

Kumar, R.,Lovell, S.,Matsumura, H.,Battaile, K.P.,Moenne-Loccoz, P.,Rivera, M.
The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change.
Biochemistry, 52:2705-2707, 2013

PubMed Abstract: Hemophores from Serratia marcescens (HasA(sm)) and Pseudomonas aeruginosa (HasA(p)) bind hemin between two loops, which harbor the axial ligands H32 and Y75. Hemin binding to the Y75 loop triggers closing of the H32 loop and enables binding of H32. Because Yersinia pestis HasA (HasA(yp)) presents a Gln at position 32, we determined the structures of apo- and holo-HasA(yp). Surprisingly, the Q32 loop in apo-HasA(yp) is already in the closed conformation, but no residue from the Q32 loop binds hemin in holo-HasA(yp). In agreement with the minimal reorganization between the apo- and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements.

PubMed: 23578210
DOI: 10.1021/bi400280z

実験手法

X-RAY DIFFRACTION (1.1 Å)