2AVK
met-azido-DcrH-Hr
Summary for 2AVK
| Entry DOI | 10.2210/pdb2avk/pdb |
| Descriptor | hemerythrin-like domain protein DcrH, SULFATE ION, MONOAZIDO-MU-OXO-DIIRON, ... (4 entities in total) |
| Functional Keywords | hemerythrin-like oxygen sensor, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Desulfovibrio vulgaris |
| Total number of polymer chains | 1 |
| Total formula weight | 16424.05 |
| Authors | Isaza, C.E.,Silaghi-Dumitrescu, R.,Iyer, R.B.,Kurtz, D.M.,Chan, M.K. (deposition date: 2005-08-30, release date: 2006-08-08, Last modification date: 2024-02-14) |
| Primary citation | Isaza, C.E.,Silaghi-Dumitrescu, R.,Iyer, R.B.,Kurtz, D.M.,Chan, M.K. Structural Basis for O(2) Sensing by the Hemerythrin-like Domain of a Bacterial Chemotaxis Protein: Substrate Tunnel and Fluxional N Terminus. Biochemistry, 45:9023-9031, 2006 Cited by PubMed Abstract: The methyl-accepting chemotaxis protein, DcrH, from the anaerobic sulfate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), has a hemerythrin-like domain, DcrH-Hr, at its C terminus. DcrH-Hr was previously shown to contain a diiron site that binds O2, suggesting an O2-sensing function. X-ray crystal structures of diferric (met-), azido-diferric (azidomet-), and diferrous (deoxy-) DcrH-Hr reveal a "substrate tunnel" distinct from that in invertebrate hemerythrins. This tunnel is proposed to facilitate the rapid autoxidation of oxy-DcrH-Hr and suggests that sensing is triggered by O2 binding and subsequent oxidation of the diferrous active site. The N-terminal loop of DcrH-Hr is highly ordered in both met- and azidomet-DcrH-Hr but is disordered in deoxy-DcrH-Hr. These redox-dependent conformational differences presumably transduce the sensory signal of DcrH-Hr to the neighboring methylation domain in the full-length receptor. Given the putative cytoplasmic localization of its Hr-like O2-sensing domain, DcrH is proposed to serve a role in negative aerotaxis (anaerotaxis). PubMed: 16866347DOI: 10.1021/bi0607812 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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