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Crystal Structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA Dehydratase Component A

Locher, Kaspar P. and Hans, Marcus and Yeh, Andrew P. and Schmid, Benedikt and Buckel, Wolfgang and Rees, Douglas C. (2001) Crystal Structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA Dehydratase Component A. Journal of Molecular Biology, 307 (1). pp. 297-308. ISSN 0022-2836. https://resolver.caltech.edu/CaltechAUTHORS:20150108-153550607

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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 Å 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.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1006/jmbi.2000.4496DOIArticle
http://www.sciencedirect.com/science/article/pii/S0022283600944966PublisherArticle
ORCID:
AuthorORCID
Rees, Douglas C.0000-0003-4073-1185
Contact Email Address:phoebe@caltech.edu
Additional Information:© 2001 Academic Press. Received 12 December 2000; received in revised form 25 January 2001; accepted 25 January 2001. We thank J. B. Howard for stimulating discussions and National Institutes of Health grant GM45162 to D.C.R. and Deutsche Forschungsgemeinschaft grants to W. B. and to M.H. for support of this research.
Funders:
Funding AgencyGrant Number
NIHGM45162
Deutsche Forschungsgemeinschaft (DFG)UNSPECIFIED
Subject Keywords:actin fold; hexokinase; heat shock protein 70; ATP hydrolysis; electron transfer
Issue or Number:1
Record Number:CaltechAUTHORS:20150108-153550607
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150108-153550607
Official Citation:Kaspar P Locher, Marcus Hans, Andrew P Yeh, Benedikt Schmid, Wolfgang Buckel, Douglas C Rees, Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A, Journal of Molecular Biology, Volume 307, Issue 1, 16 March 2001, Pages 297-308, ISSN 0022-2836, http://dx.doi.org/10.1006/jmbi.2000.4496. (http://www.sciencedirect.com/science/article/pii/S0022283600944966)
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53406
Collection:CaltechAUTHORS
Deposited By: SWORD User
Deposited On:08 Feb 2015 06:40
Last Modified:03 Oct 2019 07:49

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