2c7y

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[[Image:2c7y.gif|left|200px]]
[[Image:2c7y.gif|left|200px]]
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{{Structure
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|PDB= 2c7y |SIZE=350|CAPTION= <scene name='initialview01'>2c7y</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_2c7y", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </span>
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{{STRUCTURE_2c7y| PDB=2c7y | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c7y OCA], [http://www.ebi.ac.uk/pdbsum/2c7y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c7y RCSB]</span>
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'''PLANT ENZYME'''
'''PLANT ENZYME'''
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[[Category: Sundaramoorthy, R.]]
[[Category: Sundaramoorthy, R.]]
[[Category: 3-ketoacylcoa thiolase]]
[[Category: 3-ketoacylcoa thiolase]]
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[[Category: acyltransferase]]
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[[Category: Acyltransferase]]
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[[Category: fatty acid metabolism]]
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[[Category: Fatty acid metabolism]]
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[[Category: lipid synthesis]]
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[[Category: Lipid synthesis]]
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[[Category: oxylipin synthesis]]
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[[Category: Oxylipin synthesis]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:24:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:41 2008''
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Revision as of 18:24, 3 May 2008

Image:2c7y.gif

Template:STRUCTURE 2c7y

PLANT ENZYME


Overview

Crystal structures of peroxisomal Arabidopsis thaliana 3-ketoacyl-CoA thiolase (AtKAT), an enzyme of fatty acid beta-oxidation, are reported. The subunit, a typical thiolase, is a combination of two similar alpha/beta domains capped with a loop domain. The comparison of AtKAT with the Saccharomyces cerevisiae homologue (ScKAT) structure reveals a different placement of subunits within the functional dimers and that a polypeptide segment forming an extended loop around the open catalytic pocket of ScKAT converts to alpha-helix in AtKAT, and occludes the active site. A disulfide is formed between Cys192, on this helix, and Cys138, a catalytic residue. Access to Cys138 is determined by the structure of this polypeptide segment. AtKAT represents an oxidized, previously unknown inactive form, whilst ScKAT is the reduced and active enzyme. A high level of sequence conservation is observed, including Cys192, in eukaryotic peroxisomal, but not mitochondrial or prokaryotic KAT sequences, for this labile loop/helix segment. This indicates that KAT activity in peroxisomes is influenced by a disulfide/dithiol change linking fatty acid beta-oxidation with redox regulation.

About this Structure

2C7Y is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

The crystal structure of a plant 3-ketoacyl-CoA thiolase reveals the potential for redox control of peroxisomal fatty acid beta-oxidation., Sundaramoorthy R, Micossi E, Alphey MS, Germain V, Bryce JH, Smith SM, Leonard GA, Hunter WN, J Mol Biol. 2006 Jun 2;359(2):347-57. Epub 2006 Mar 29. PMID:16630629 Page seeded by OCA on Sat May 3 21:24:57 2008

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