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PMID: 2726740 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 86 ·No. 10 ·1989-05-00 ·Pages 3639-43

Robbins AH, Stout CD

Abstract

The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC 4.2.1.3] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual of 18.2%. Comparison of this structure to the recently determined 2.1-A resolution structure of the inactive enzyme containing a [3Fe-4S] cluster, by difference Fourier analysis, shows that upon activation iron is inserted into the structure isomorphously. The common atoms of the [3Fe-4S] and [4Fe-4S] cores agree within 0.1 A; the three common cysteinyl S gamma ligand atoms agree within 0.25 A. The fourth ligand of the Fe inserted into the [3Fe-4S] cluster is a water or hydroxyl from solvent, consistent with the absence of a free cysteine ligand in the enzyme active site cleft and the isomorphism of the two structures. A water molecule occupies a similar site in the crystal structure of the inactive enzyme.

MeSH Terms
Aconitate Hydratase Animals Binding Sites Enzyme Activation Iron-Sulfur Proteins/ultrastructure Metalloproteins/ultrastructure Models, Molecular Myocardium/enzymology Protein Conformation Swine X-Ray Diffraction
Chemicals
Iron-Sulfur Proteins Metalloproteins Aconitate Hydratase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Robbins A H
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Stout C D
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31 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.86.10.3639
Published
1989-05-00
Pages
3639-43
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC287193
Subset
IM
Grants
NIGMS NIH HHS · GM-36325 · United States
External Links
PubMed source DOI: 10.1073/pnas.86.10.3639 PMC Full Text View journal details
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