2awc

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{{STRUCTURE_2awc| PDB=2awc | SCENE= }}
{{STRUCTURE_2awc| PDB=2awc | SCENE= }}
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'''deoxy-DcrH-Hr'''
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===deoxy-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).
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{{ABSTRACT_PUBMED_16866347}}
==About this Structure==
==About this Structure==
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[[Category: Silaghi-Dumitrescu, R.]]
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[[Category: Four helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:39:02 2008''

Revision as of 15:39, 27 July 2008

Image:2awc.png

Template:STRUCTURE 2awc

deoxy-DcrH-Hr

Template:ABSTRACT PUBMED 16866347

About this Structure

2AWC is a Single protein structure of sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.

Reference

Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N terminus., Isaza CE, Silaghi-Dumitrescu R, Iyer RB, Kurtz DM Jr, Chan MK, Biochemistry. 2006 Aug 1;45(30):9023-31. PMID:16866347

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