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2AWY

met-DcrH-Hr

Summary for 2AWY
Entry DOI10.2210/pdb2awy/pdb
Descriptorhemerythrin-like domain protein DcrH, CHLORIDE ION, CALCIUM ION, ... (5 entities in total)
Functional Keywordshemerythrin-like oxygen sensor, oxygen storage-transport complex, oxygen storage/transport
Biological sourceDesulfovibrio vulgaris
Total number of polymer chains2
Total formula weight32682.93
Authors
Isaza, C.E.,Silaghi-Dumitrescu, R.,Iyer, R.B.,Kurtz, D.M.,Chan, M.K. (deposition date: 2005-09-02, release date: 2006-08-15, Last modification date: 2024-02-14)
Primary citationIsaza, 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: 16866347
DOI: 10.1021/bi0607812
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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数据于2025-07-30公开中

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