1HUX

CRYSTAL STRUCTURE OF THE ACIDAMINOCOCCUS FERMENTANS (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE COMPONENT A

Summary for 1HUX

• Entry DOI: 10.2210/pdb1hux/pdb
• Descriptor: ACTIVATOR OF (R)-2-HYDROXYGLUTARYL-COA DEHYDRATASE, IRON/SULFUR CLUSTER, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: actin fold, metal binding protein
• Biological source: Acidaminococcus fermentans
• Total number of polymer chains: 2
• Total formula weight: 58209.51

Authors

Locher, K.P.,Hans, M.,Yeh, A.P.,Schmid, B.,Buckel, W.,Rees, D.C. (deposition date: 2001-01-04, release date: 2001-03-21, Last modification date: 2024-02-07)

Primary citation

Locher, K.P.,Hans, M.,Yeh, A.P.,Schmid, B.,Buckel, W.,Rees, D.C.
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A.
J.Mol.Biol., 307:297-308, 2001

PubMed Abstract: 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.

PubMed: 11243821
DOI: 10.1006/jmbi.2000.4496

Experimental method

X-RAY DIFFRACTION (3 Å)