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The hemophore HasA from Yersinia pestis (HasAyp) coordinates hemin with a single residue, Tyr75, and with minimal conformational change.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kumar R,Lovell S,Matsumura H,Battaile KP,Moënne-Loccoz P,Rivera M

doi

10.1021/bi400280z

subject

Has Abstract

pub_date

2013-04-23 00:00:00

pages

2705-7

issue

16

eissn

0006-2960

issn

1520-4995

journal_volume

52

pub_type

杂志文章

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