1ndi
From Proteopedia
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|PDB= 1ndi |SIZE=350|CAPTION= <scene name='initialview01'>1ndi</scene>, resolution 2.30Å | |PDB= 1ndi |SIZE=350|CAPTION= <scene name='initialview01'>1ndi</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene> | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnitine_O-acetyltransferase Carnitine O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.7 2.3.1.7] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ndb|1NDB]], [[1ndf|1NDF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ndi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ndi OCA], [http://www.ebi.ac.uk/pdbsum/1ndi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ndi RCSB]</span> | ||
}} | }} | ||
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[[Category: Jogl, G.]] | [[Category: Jogl, G.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| - | [[Category: COA]] | ||
[[Category: acetyl transfer]] | [[Category: acetyl transfer]] | ||
[[Category: coa]] | [[Category: coa]] | ||
[[Category: coenzyme some]] | [[Category: coenzyme some]] | ||
| - | ''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 22:28:51 2008'' |
Revision as of 19:28, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Carnitine O-acetyltransferase, with EC number 2.3.1.7 | ||||||
| Related: | 1NDB, 1NDF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Carnitine Acetyltransferase in complex with CoA
Overview
Carnitine acyltransferases have crucial roles in the transport of fatty acids for beta-oxidation. Dysregulation of these enzymes can lead to serious diseases in humans, and they are targets for therapeutic development against diabetes. We report the crystal structures of murine carnitine acetyltransferase (CRAT), alone and in complex with its substrate carnitine or CoA. The structure contains two domains. Surprisingly, these two domains share the same backbone fold, which is also similar to that of chloramphenicol acetyltransferase and dihydrolipoyl transacetylase. The active site is located at the interface between the two domains. Carnitine and CoA are bound in deep channels in the enzyme, on opposite sides of the catalytic His343 residue. The structural information provides a molecular basis for understanding the catalysis by carnitine acyltransferases and for designing their inhibitors. Specifically, our structural information suggests that the substrate carnitine may assist the catalysis by stabilizing the oxyanion in the reaction intermediate.
About this Structure
1NDI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport., Jogl G, Tong L, Cell. 2003 Jan 10;112(1):113-22. PMID:12526798
Page seeded by OCA on Sun Mar 30 22:28:51 2008
