1b0m
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aconitate hydratase, with EC number 4.2.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACONITASE R644Q:FLUOROCITRATE COMPLEX
OverviewOverview
The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.
About this StructureAbout this Structure
1B0M is a Single protein structure of sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1ATQ. Full crystallographic information is available from OCA.
ReferenceReference
The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex., Lloyd SJ, Lauble H, Prasad GS, Stout CD, Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981
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