1b0m
From Proteopedia
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|PDB= 1b0m |SIZE=350|CAPTION= <scene name='initialview01'>1b0m</scene>, resolution 2.50Å | |PDB= 1b0m |SIZE=350|CAPTION= <scene name='initialview01'>1b0m</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene> | + | |LIGAND= <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0m OCA], [http://www.ebi.ac.uk/pdbsum/1b0m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0m RCSB]</span> | ||
}} | }} | ||
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[[Category: Prasad, G S.]] | [[Category: Prasad, G S.]] | ||
[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
- | [[Category: FLC]] | ||
- | [[Category: SF4]] | ||
[[Category: aconitase r644q]] | [[Category: aconitase r644q]] | ||
[[Category: fluorocitrate complex]] | [[Category: fluorocitrate complex]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
- | ''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 18:51:28 2008'' |
Revision as of 15:51, 30 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | , | ||||||
Activity: | Aconitate hydratase, with EC number 4.2.1.3 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ACONITASE R644Q:FLUOROCITRATE COMPLEX
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
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.
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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