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| [[Image:2avk.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2avk| PDB=2avk | SCENE= }} | | {{STRUCTURE_2avk| PDB=2avk | SCENE= }} |
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| '''met-azido-DcrH-Hr'''
| | ===met-azido-DcrH-Hr=== |
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| ==Overview==
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| 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). | | The line below this paragraph, {{ABSTRACT_PUBMED_16866347}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16866347 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16866347}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Silaghi-Dumitrescu, R.]] | | [[Category: Silaghi-Dumitrescu, R.]] |
| [[Category: Hemerythrin-like oxygen sensor]] | | [[Category: Hemerythrin-like oxygen sensor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:31:31 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:28:07 2008'' |
