Structural highlights
Publication Abstract from PubMed
Hemophores from Serratia marcescens (HasAsm) and Pseudomonas aeruginosa (HasAp) 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 (HasAyp) presents a Gln at position 32, we determined the structures of apo- and holo-HasAyp. Surprisingly, the Q32 loop in apo-HasAyp is already in the closed conformation, but no residue from the Q32 loop binds hemin in holo-HasAyp. 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.
The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change.,Kumar R, Lovell S, Matsumura H, Battaile KP, Moenne-Loccoz P, Rivera M Biochemistry. 2013 Apr 23;52(16):2705-7. doi: 10.1021/bi400280z. Epub 2013 Apr, 11. PMID:23578210[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumar R, Lovell S, Matsumura H, Battaile KP, 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. 2013 Apr 23;52(16):2705-7. doi: 10.1021/bi400280z. Epub 2013 Apr, 11. PMID:23578210 doi:10.1021/bi400280z
