1b0m

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ACONITASE R644Q:FLUOROCITRATE COMPLEX

Structural highlights

1b0m is a 1 chain structure with sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1atq. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:FLC, SF4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACON_PIG Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
4 reviews cite this structure
Gutteridge et al. (2005)
No citations found

See Also

References

  1. Lloyd SJ, Lauble H, Prasad GS, Stout CD. The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex. Protein Sci. 1999 Dec;8(12):2655-62. PMID:10631981

Contents


PDB ID 1b0m

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