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5it1

From Proteopedia

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<StructureSection load='5it1' size='340' side='right'caption='[[5it1]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5it1' size='340' side='right'caption='[[5it1]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5it1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1799 As 4.1799]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IT1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IT1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5it1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_peucetius Streptomyces peucetius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IT1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OH:4,4-PROPANE-2,2-DIYLDIPHENOL'>2OH</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp7863 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1950 AS 4.1799])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2OH:4,4-PROPANE-2,2-DIYLDIPHENOL'>2OH</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5it1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5it1 OCA], [https://pdbe.org/5it1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5it1 RCSB], [https://www.ebi.ac.uk/pdbsum/5it1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5it1 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5it1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5it1 OCA], [http://pdbe.org/5it1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5it1 RCSB], [http://www.ebi.ac.uk/pdbsum/5it1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5it1 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q70AS3_STRPE Q70AS3_STRPE]
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Cytochrome P450 monooxygenases (CYP, EC 1.14.14.1) belong to a large family of enzymes that catalyze the hydroxylation of various substrates. Here, we present the crystal structure of CYP105P2 isolated from Streptomyces peucetius ATCC27952 at a 2.1 A resolution. The structure shows the presence of a pseudo-ligand molecule in the active site, which was co-purified fortuitously and is presumed to be a biphenyl derivative. Comparison with previously determined substrate-bound CYP structures showed that binding of the ligand produces large and distinctive conformational changes in alpha2-alpha3, alpha7-alpha9, and the C-terminal loop regions. This structural flexibility confirms our previous observation that CYP105P2 can accommodate a broad range of ligands. The structure complexed with a pseudo-ligand provides the first molecular view of CYP105P2-ligand interactions, and it indicates the involvement of hydrophobic residues (Pro82, Ala181, Met187, Leu189, Leu193, and Ile236) in the interactions between hydrophobic ligands and CYP105P2. These results provide useful insights into the structural changes involved in the recognition of different ligands by CYP105P2.
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Crystal Structure of Cytochrome P450 (CYP105P2) from Streptomyces peucetius and Its Conformational Changes in Response to Substrate Binding.,Lee CW, Lee JH, Rimal H, Park H, Lee JH, Oh TJ Int J Mol Sci. 2016 May 25;17(6). pii: E813. doi: 10.3390/ijms17060813. PMID:27231902<ref>PMID:27231902</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5it1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: As 4 1799]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Unspecific monooxygenase]]
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[[Category: Streptomyces peucetius]]
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[[Category: Lee, C W]]
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[[Category: Lee CW]]
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[[Category: Lee, J H]]
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[[Category: Lee JH]]
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[[Category: Cyp105p2-biphenyl compound complex]]
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[[Category: Oxidoreductase]]
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Current revision

Streptomyces peucetius CYP105P2 complex with biphenyl compound

PDB ID 5it1

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