1b0k

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|PDB= 1b0k |SIZE=350|CAPTION= <scene name='initialview01'>1b0k</scene>, resolution 2.50&Aring;
|PDB= 1b0k |SIZE=350|CAPTION= <scene name='initialview01'>1b0k</scene>, resolution 2.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=O:OXYGEN ATOM'>O</scene>
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|LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0k OCA], [http://www.ebi.ac.uk/pdbsum/1b0k PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0k RCSB]</span>
}}
}}
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[[Category: Prasad, G S.]]
[[Category: Prasad, G S.]]
[[Category: Stout, C D.]]
[[Category: Stout, C D.]]
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[[Category: FLC]]
 
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[[Category: O]]
 
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[[Category: SF4]]
 
[[Category: iron-sulfur]]
[[Category: iron-sulfur]]
[[Category: lyase]]
[[Category: lyase]]
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[[Category: tricarboxylic acid cycle]]
[[Category: tricarboxylic acid cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:17 2008''

Revision as of 15:51, 30 March 2008


PDB ID 1b0k

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands: , ,
Activity: Aconitate hydratase, with EC number 4.2.1.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



S642A:FLUOROCITRATE COMPLEX OF ACONITASE


Overview

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 Structure

1B0K is a Single protein structure of sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1AS9. Full crystallographic information is available from OCA.

Reference

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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