1hux
From Proteopedia
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|PDB= 1hux |SIZE=350|CAPTION= <scene name='initialview01'>1hux</scene>, resolution 3.0Å | |PDB= 1hux |SIZE=350|CAPTION= <scene name='initialview01'>1hux</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HGDC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=905 Acidaminococcus fermentans]) | |GENE= HGDC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=905 Acidaminococcus fermentans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hux OCA], [http://www.ebi.ac.uk/pdbsum/1hux PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hux RCSB]</span> | ||
}} | }} | ||
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[[Category: Schmid, B.]] | [[Category: Schmid, B.]] | ||
[[Category: Yeh, A P.]] | [[Category: Yeh, A P.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: SF4]] | ||
[[Category: actin fold]] | [[Category: actin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:45 2008'' |
Revision as of 18:10, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | HGDC (Acidaminococcus fermentans) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A
Overview
Acidaminococcus fermentans degrades glutamate via the hydroxyglutarate pathway, which involves the syn-elimination of water from (R)-2-hydroxyglutaryl-CoA in a key reaction of the pathway. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. Component A (CompA), a homodimeric protein of 2x27 kDa, contains a single, bridging [4Fe-4S] cluster and uses the hydrolysis of ATP to deliver an electron to the dehydratase component (CompD), where the electron is used catalytically. The structure of the extremely oxygen-sensitive CompA protein was solved by X-ray crystallography to 3 A resolution. The protein was found to be a member of the actin fold family, revealing a similar architecture and nucleotide-binding site. The key differences between CompA and other members of the actin fold family are: (i) the presence of a cluster binding segment, the "cluster helix"; (ii) the [4Fe-4S] cluster; and (iii) the location of the homodimer interface, which involves the bridging cluster. Possible reaction mechanisms are discussed in light of the close structural similarity to members of the actin-fold family and the functional similarity to the nitrogenase Fe- protein.
About this Structure
1HUX is a Single protein structure of sequence from Acidaminococcus fermentans. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A., Locher KP, Hans M, Yeh AP, Schmid B, Buckel W, Rees DC, J Mol Biol. 2001 Mar 16;307(1):297-308. PMID:11243821
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