The structure of aconitase

  title={The structure of aconitase},
  author={Arthur Robbins and Charles David Stout},
  journal={Proteins: Structure},
The crystal structure of the 80,000 Da FeS enzyme aconitase has been solved and refined at 2.1 Å resolution. The protein contains four domains; the first three from the N‐terminus are closely associated around the [3Fe–4S] cluster with all three cysteine ligands to the cluster being provided by the third domain. Associationof the larger C‐terminal domain with the first three domains createsan extensive cleft leading to the FeS cluster. Residues from all four domains contribute to the active… 

Crystal structures of aconitase with isocitrate and nitroisocitrate bound.

The crystal structures of mitochondrial aconitase with isocitrate and nitroisocitrate bound have been solved and refined to R factors of 0.179 and 0.161, respectively, for all observed data in the

Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis

The crystal structure of LeuD was shown to be compatible with the solution X‐ray scattering data from the small subunit, and solution scattering results suggest that the large subunit LeuC and the LeuCD complex have overall shapes, which are radically different from the ones observed in the crystals of the functional homolog mitochondrial aconitase.

E. coli aconitase B structure reveals a HEAT-like domain with implications for protein–protein recognition

The 2.4 Å structure of E. coli AcnB reveals a high degree of conservation at the active site despite its domain reorganization, and reveals that the additional domain, characteristic of theAcnB subfamily, is a HEAT-like domain, implying a role in protein–protein recognition.

Conservation of aconitase residues revealed by multiple sequence analysis. Implications for structure/function relationships.

This work has aligned 28 members of the Fe-S isomerase family, identified highly conserved amino acid residues, and integrated this information with data on the crystallographic structure of mammalian mitochondrial aconitase to propose structural and/or functional roles for the previously unrecognized conserved residues.

Engineering of protein bound iron‐sulfur clusters

An increasing number of iron-sulfur (Fe-S) proteins are found in which the Fe-S cluster is not involved in net electron transfer, as it is in the majority of Fe-S proteins. Most of the former are

Crystallographic structure and functional implications of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii

The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined and structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre.



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

  • A. RobbinsC. Stout
  • Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1989
The structure of activated pig heart aconitase [citrate(isocitrate) hydro-lyase, EC] containing a [4Fe-4S] cluster has been refined at 2.5-A resolution to a crystallographic residual of

The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases. X-ray refinement of cytoplasmic malate dehydrogenase.

Using x-ray phases based on the refined coordinates, analysis of the resultant electron density maps has led to a new model of cytoplasmic malate dehydrogenase and a tentative "x-ray sequence" of the dimeric enzyme.

Mode of substrate carboxyl binding to the [4Fe-4S]+ cluster of reduced aconitase as studied by 17O and 13C electron-nuclear double resonance spectroscopy.

It is concluded that, on addition of any one of the three substrates, cis-aconsitate is the predominant species bound to Fea of the cluster along with solvent HxO and that cis-aconitate is bound in the citrate mode (carboxyl at C-2).