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The structure of aconitase.

A H Robbins1, C D Stout

  • 1Research Institute of Scripps Clinic, La Jolla, California 92037.

Proteins
|January 1, 1989
PubMed
Summary

The crystal structure of the iron-sulfur (Fe-S) enzyme aconitase was determined at 2.1 A resolution. This reveals its four-domain structure, active site, and the [3Fe-4S] cluster crucial for its function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Aconitase is an 80,000 Da iron-sulfur (Fe-S) enzyme.
  • Understanding its structure is key to elucidating its catalytic mechanism.

Purpose of the Study:

  • To determine the high-resolution crystal structure of aconitase.
  • To characterize the protein's domain organization and active site.

Main Methods:

  • X-ray crystallography
  • Structure refinement at 2.1 A resolution

Main Results:

  • The 80,000 Da Fe-S enzyme aconitase structure was solved and refined.
  • The protein comprises four domains with the [3Fe-4S] cluster ligated by the third domain.
  • An extensive cleft leads to the active site, defined by the Fe-S cluster and a bound sulfate (SO4(2-)) ion.

Conclusions:

  • The structure reveals intricate domain associations around the [3Fe-4S] cluster.
  • Active site residues, including Arg, His, Ser, Asp, Glu, Asn, and Gln, are identified.
  • The sulfate ion binding site provides insights into substrate/inhibitor interactions.

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