2ve3
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ve3' size='340' side='right'caption='[[2ve3]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2ve3' size='340' side='right'caption='[[2ve3]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ve3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2ve3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VE3 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]] 2.1Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=REA:RETINOIC+ACID'>REA</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=2ve3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ve3 OCA], [https://pdbe.org/2ve3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ve3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ve3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ve3 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=2ve3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ve3 OCA], [https://pdbe.org/2ve3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ve3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ve3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ve3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CP120_SYNY3 CP120_SYNY3] | ||
== 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=2ve3 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=2ve3 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structures of substrate-free and all- trans-retinoic acid-bound CYP120A1 from Synechocystis sp. PCC 6803 were determined at 2.4 and 2.1 A resolution, respectively, representing the first structural characterization of a cyanobacterial P450. Features of CYP120A1 not observed in other P450 structures include an aromatic ladder flanking the channel leading to the active site and a triple-glycine motif within SRS5. Using spectroscopic methods, CYP120A1 is shown to bind 13- cis-retinoic acid, 9- cis-retinoic acid, and retinal with high affinity and dissociation constants of less than 1 microM. Metabolism of retinoic acid by CYP120A1 suggests that CYP120A1 hydroxylates a variety of retinoid derivatives in vivo. On the basis of the retinoic acid-bound CYP120A1 crystal structure, we propose that either carbon 2 or the methyl groups (C16 or C17) of the beta-ionone ring are modified by CYP120A1. | ||
| - | |||
| - | Crystal Structures of Substrate-Free and Retinoic Acid-Bound Cyanobacterial Cytochrome P450 CYP120A1.,Kuhnel K, Ke N, Cryle MJ, Sligar SG, Schuler MA, Schlichting I Biochemistry. 2008 May 31. PMID:18512957<ref>PMID:18512957</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2ve3" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ke | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Kuhnel | + | [[Category: Ke N]] |
| - | [[Category: Schlichting | + | [[Category: Kuhnel K]] |
| - | [[Category: Schuler | + | [[Category: Schlichting I]] |
| - | [[Category: Sligar | + | [[Category: Schuler MA]] |
| - | + | [[Category: Sligar SG]] | |
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Current revision
Retinoic acid bound cyanobacterial CYP120A1
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