2h4t
From Proteopedia
(Difference between revisions)
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<StructureSection load='2h4t' size='340' side='right'caption='[[2h4t]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2h4t' size='340' side='right'caption='[[2h4t]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2h4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2h4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H4T FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D12:DODECANE'>D12</scene></td></tr> |
- | + | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4t OCA], [https://pdbe.org/2h4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h4t RCSB], [https://www.ebi.ac.uk/pdbsum/2h4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h4t ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h4t OCA], [https://pdbe.org/2h4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h4t RCSB], [https://www.ebi.ac.uk/pdbsum/2h4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h4t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CPT2_RAT CPT2_RAT] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h4t ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h4t ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Carnitine palmitoyltransferase II (CPT-II) has a crucial role in the beta-oxidation of long-chain fatty acids in mitochondria. We report here the crystal structure of rat CPT-II at 1.9A resolution. The overall structure shares strong similarity to those of short- and medium-chain carnitine acyltransferases, although detailed structural differences in the active site region have a significant impact on the substrate selectivity of CPT-II. Three aliphatic chains, possibly from a detergent that is used for the crystallization, were found in the structure. Two of them are located in the carnitine and CoA binding sites, respectively. The third aliphatic chain may mimic the long-chain acyl group in the substrate of CPT-II. The binding site for this aliphatic chain does not exist in the short- and medium-chain carnitine acyltransferases, due to conformational differences among the enzymes. A unique insert in CPT-II is positioned on the surface of the enzyme, with a highly hydrophobic surface. It is likely that this surface patch mediates the association of CPT-II with the inner membrane of the mitochondria. | ||
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- | Crystal structure of rat carnitine palmitoyltransferase II (CPT-II).,Hsiao YS, Jogl G, Esser V, Tong L Biochem Biophys Res Commun. 2006 Aug 4;346(3):974-80. Epub 2006 Jun 9. PMID:16781677<ref>PMID:16781677</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 2h4t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]] | *[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Buffalo rat]] | ||
- | [[Category: Carnitine O-palmitoyltransferase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Esser | + | [[Category: Rattus norvegicus]] |
- | [[Category: Hsiao | + | [[Category: Esser V]] |
- | [[Category: Jogl | + | [[Category: Hsiao YS]] |
- | [[Category: Tong | + | [[Category: Jogl G]] |
- | + | [[Category: Tong L]] | |
- | + |
Current revision
Crystal structure of rat carnitine palmitoyltransferase II
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