2avk
From Proteopedia
(New page: 200px<br /><applet load="2avk" size="350" color="white" frame="true" align="right" spinBox="true" caption="2avk, resolution 1.530Å" /> '''met-azido-DcrH-Hr''...) |
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==Overview== | ==Overview== | ||
| - | The methyl-accepting chemotaxis protein, DcrH, from the anaerobic | + | 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). |
==About this Structure== | ==About this Structure== | ||
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[[Category: Desulfovibrio vulgaris]] | [[Category: Desulfovibrio vulgaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chan, M | + | [[Category: Chan, M K.]] |
| - | [[Category: Isaza, C | + | [[Category: Isaza, C E.]] |
| - | [[Category: Iyer, R | + | [[Category: Iyer, R B.]] |
| - | [[Category: Kurtz, D | + | [[Category: Kurtz, D M.]] |
[[Category: Silaghi-Dumitrescu, R.]] | [[Category: Silaghi-Dumitrescu, R.]] | ||
[[Category: FEA]] | [[Category: FEA]] | ||
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[[Category: hemerythrin-like oxygen sensor]] | [[Category: hemerythrin-like oxygen sensor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:31:32 2008'' |
Revision as of 14:31, 21 February 2008
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met-azido-DcrH-Hr
Overview
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).
About this Structure
2AVK is a Single protein structure of sequence from Desulfovibrio vulgaris with and as ligands. 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
Page seeded by OCA on Thu Feb 21 16:31:32 2008
