2avk
From Proteopedia
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|PDB= 2avk |SIZE=350|CAPTION= <scene name='initialview01'>2avk</scene>, resolution 1.530Å | |PDB= 2avk |SIZE=350|CAPTION= <scene name='initialview01'>2avk</scene>, resolution 1.530Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FEA:MONOAZIDO-MU-OXO-DIIRON'>FEA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= locus AF210632 accession AF210632.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=881 Desulfovibrio vulgaris]) | |GENE= locus AF210632 accession AF210632.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=881 Desulfovibrio vulgaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2avk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2avk OCA], [http://www.ebi.ac.uk/pdbsum/2avk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2avk RCSB]</span> | ||
}} | }} | ||
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[[Category: Kurtz, D M.]] | [[Category: Kurtz, D M.]] | ||
[[Category: Silaghi-Dumitrescu, R.]] | [[Category: Silaghi-Dumitrescu, R.]] | ||
| - | [[Category: FEA]] | ||
| - | [[Category: SO4]] | ||
[[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 Mon Mar 31 01:57:48 2008'' |
Revision as of 22:57, 30 March 2008
| |||||||
| , resolution 1.530Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | locus AF210632 accession AF210632.1 (Desulfovibrio vulgaris) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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