4JER
1.1A resolution Apo structure of the hemophore HasA from Yersinia pestis (Tetragonal Form)
Summary for 4JER
| Entry DOI | 10.2210/pdb4jer/pdb |
| Related | 4JES 4JET |
| Descriptor | Hemophore HasA, SODIUM ION (3 entities in total) |
| Functional Keywords | heme binding protein, transport protein |
| Biological source | Yersinia pestis |
| Total number of polymer chains | 1 |
| Total formula weight | 21048.08 |
| Authors | Kumar, R.,Lovell, S.,Battaile, K.P.,Rivera, M. (deposition date: 2013-02-27, release date: 2013-04-24, Last modification date: 2023-09-20) |
| Primary citation | 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 Cited by 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: 23578210DOI: 10.1021/bi400280z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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