1c97
From Proteopedia
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|PDB= 1c97 |SIZE=350|CAPTION= <scene name='initialview01'>1c97</scene>, resolution 1.98Å | |PDB= 1c97 |SIZE=350|CAPTION= <scene name='initialview01'>1c97</scene>, resolution 1.98Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</scene>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> |
| - | |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] | + | |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= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1c96|1C96]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c97 OCA], [http://www.ebi.ac.uk/pdbsum/1c97 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c97 RCSB]</span> | ||
}} | }} | ||
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[[Category: Prasad, G S.]] | [[Category: Prasad, G S.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
| - | [[Category: ICT]] | ||
| - | [[Category: O]] | ||
| - | [[Category: SF4]] | ||
[[Category: 3d-structure]] | [[Category: 3d-structure]] | ||
[[Category: 4fe-4]] | [[Category: 4fe-4]] | ||
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[[Category: tricarboxylic acid cycle]] | [[Category: tricarboxylic acid cycle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:12 2008'' |
Revision as of 16:17, 30 March 2008
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| , resolution 1.98Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Aconitate hydratase, with EC number 4.2.1.3 | ||||||
| Related: | 1C96
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
S642A:ISOCITRATE 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
1C97 is a Single protein structure of sequence from Bos taurus. 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
Page seeded by OCA on Sun Mar 30 19:17:12 2008
