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| [[Image:2c7z.gif|left|200px]] | | {{Seed}} |
| | [[Image:2c7z.png|left|200px]] |
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| {{STRUCTURE_2c7z| PDB=2c7z | SCENE= }} | | {{STRUCTURE_2c7z| PDB=2c7z | SCENE= }} |
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| '''PLANT ENZYME CRYSTAL FORM II'''
| | ===PLANT ENZYME CRYSTAL FORM II=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16630629}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16630629 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16630629}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxylipin synthesis]] | | [[Category: Oxylipin synthesis]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:25:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:21:38 2008'' |
