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Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal.
Proc Natl Acad Sci U S A. 1989 May; 86(10):3639-43.PN

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.

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Authors+Show Affiliations

Robbins AH
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Stout CD
No affiliation info available

MeSH

Aconitate HydrataseAnimalsBinding SitesEnzyme ActivationIron-Sulfur ProteinsMetalloproteinsModels, MolecularMyocardiumProtein ConformationSwineX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

2726740

Citation

Robbins, A H., and C D. Stout. "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, pp. 3639-43.
Robbins AH, Stout CD. Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. Proc Natl Acad Sci U S A. 1989;86(10):3639-43.
Robbins, A. H., & Stout, C. D. (1989). 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, 86(10), 3639-43.
Robbins AH, Stout CD. Structure of Activated Aconitase: Formation of the [4Fe-4S] Cluster in the Crystal. Proc Natl Acad Sci U S A. 1989;86(10):3639-43. PubMed PMID: 2726740.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of activated aconitase: formation of the [4Fe-4S] cluster in the crystal. AU - Robbins,A H, AU - Stout,C D, PY - 1989/5/1/pubmed PY - 1989/5/1/medline PY - 1989/5/1/entrez SP - 3639 EP - 43 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 86 IS - 10 N2 - 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. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/2726740/Structure_of_activated_aconitase:_formation_of_the_[4Fe_4S]_cluster_in_the_crystal_ DB - PRIME DP - Unbound Medicine ER -