2c7y: Difference between revisions
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='2c7y' size='340' side='right' caption='[[2c7y]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2c7y' size='340' side='right' caption='[[2c7y]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c7y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2c7y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C7Y FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c7z|2c7z]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c7z|2c7z]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2c7y RCSB], [http://www.ebi.ac.uk/pdbsum/2c7y PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2c7y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c7y RCSB], [http://www.ebi.ac.uk/pdbsum/2c7y PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 27: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2c7y" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 35: | Line 36: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acetyl-CoA C-acyltransferase]] | [[Category: Acetyl-CoA C-acyltransferase]] | ||
[[Category: | [[Category: Arath]] | ||
[[Category: Alphey, M S]] | [[Category: Alphey, M S]] | ||
[[Category: Bryce, J H]] | [[Category: Bryce, J H]] | ||
Revision as of 10:54, 11 September 2015
PLANT ENZYMEPLANT ENZYME
Structural highlights
Function[THIK2_ARATH] Involved in long chain fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Confers sensitivity to 2,4-dichlorophenoxybutiric acid (2,4-DB). Required for local and systemic induction of jasmonic acid (JA) biosynthesis after wounding. Seems to be involved in JA biosynthesis during senescence.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCrystal 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 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[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||