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2awy
From Proteopedia
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| - | [[Image:2awy.gif|left|200px]] | + | [[Image:2awy.gif|left|200px]] |
| - | + | ||
| - | '''met-DcrH-Hr''' | + | {{Structure |
| + | |PDB= 2awy |SIZE=350|CAPTION= <scene name='initialview01'>2awy</scene>, resolution 2.100Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''met-DcrH-Hr''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AWY is a [ | + | 2AWY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AWY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16866347 16866347] |
[[Category: Desulfovibrio vulgaris]] | [[Category: Desulfovibrio vulgaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:54:52 2008'' |
Revision as of 13:54, 20 March 2008
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| , resolution 2.100Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
met-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
2AWY 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
Page seeded by OCA on Thu Mar 20 15:54:52 2008
