1c96 | pdb_00001c96

S642A:CITRATE COMPLEX OF ACONITASE

spinqualitylabelsall models 1c96, resolution 1.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1c96 is a 1 chain structure with sequence from Bos taurus. The May 2007 RCSB PDB Molecule of the Month feature on Aconitase and Iron Regulatory Protein 1 by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.81Å Ligands: FLC, O Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACON_BOVIN 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aconitase 3D structures

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