2c7y

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[[Image:2c7y.gif|left|200px]]<br /><applet load="2c7y" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c7y.gif|left|200px]]
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caption="2c7y, resolution 2.10&Aring;" />
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'''PLANT ENZYME'''<br />
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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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|SITE=
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|LIGAND=
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|ACTIVITY= [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]
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|GENE=
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}}
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'''PLANT ENZYME'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C7Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7Y OCA].
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2C7Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7Y OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16630629 16630629]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16630629 16630629]
[[Category: Acetyl-CoA C-acyltransferase]]
[[Category: Acetyl-CoA C-acyltransferase]]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:01 2008''

Revision as of 14:12, 20 March 2008

Image:2c7y.gif


PDB ID 2c7y

Drag the structure with the mouse to rotate
, resolution 2.10Å
Activity: Acetyl-CoA C-acyltransferase, with EC number 2.3.1.16
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 16:12:01 2008

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