1ndb: Difference between revisions
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[[Image:1ndb.gif|left|200px]] | [[Image:1ndb.gif|left|200px]] | ||
'''Crystal structure of Carnitine Acetyltransferase''' | {{Structure | ||
|PDB= 1ndb |SIZE=350|CAPTION= <scene name='initialview01'>1ndb</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of Carnitine Acetyltransferase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NDB is a [ | 1NDB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDB OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12526798 12526798] | ||
[[Category: Carnitine O-acetyltransferase]] | [[Category: Carnitine O-acetyltransferase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: acetyl transfer]] | [[Category: acetyl transfer]] | ||
[[Category: coa]] | [[Category: coa]] | ||
[[Category: coenzyme | [[Category: coenzyme some]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:23 2008'' | ||
Revision as of 13:55, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Activity: | Carnitine O-acetyltransferase, with EC number 2.3.1.7 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Carnitine Acetyltransferase
OverviewOverview
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 StructureAbout this Structure
1NDB is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
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