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5h1z

From Proteopedia

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<StructureSection load='5h1z' size='340' side='right'caption='[[5h1z]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='5h1z' size='340' side='right'caption='[[5h1z]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5h1z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingomonas_sp._pamc_26605 Sphingomonas sp. pamc 26605]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H1Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H1Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5h1z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._PAMC_26605 Sphingomonas sp. PAMC 26605]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H1Z 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=D12:DODECANE'>D12</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]] 3.1&#8491;</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=5h1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h1z OCA], [http://pdbe.org/5h1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h1z RCSB], [http://www.ebi.ac.uk/pdbsum/5h1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h1z ProSAT]</span></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=D12:DODECANE'>D12</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=5h1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h1z OCA], [https://pdbe.org/5h1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h1z RCSB], [https://www.ebi.ac.uk/pdbsum/5h1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h1z ProSAT]</span></td></tr>
</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/A0A1S4NYE0_9SPHN A0A1S4NYE0_9SPHN]
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Enzymatic alkane hydroxylation reactions are useful for producing pharmaceutical and agricultural chemical intermediates from hydrocarbons. Several cytochrome P450 enzymes catalyze the regio- and stereo-specific hydroxylation of alkanes. We evaluated the substrate binding of a putative CYP alkane hydroxylase (CYP153D17) from the bacterium Sphingomonas sp. PAMC 26605. Substrate affinities to C10-C12 n-alkanes and C10-C14 fatty acids with Kd values varied from 0.42 to 0.59 muM. A longer alkane (C12) bound more strongly than a shorter alkane (C10), while shorter fatty acids (C10, capric acid; C12, lauric acid) bound more strongly than a longer fatty acid (C14, myristic acid). These data displayed a broad substrate specificity of CYP153D17, hence it was named as a putative CYP alkane hydroxylase. Moreover, the crystal structure of CYP153D17 was determined at 3.1 A resolution. This is the first study to provide structural information for the CYP153D family. Structural analysis showed that a co-purified alkane-like compound bound near the active-site heme group. The alkane-like substrate is in the hydrophobic pocket containing Thr74, Met90, Ala175, Ile240, Leu241, Val244, Leu292, Met295, and Phe393. Comparison with other CYP structures suggested that conformational changes in the beta1-beta2, alpha3-alpha4, and alpha6-alpha7 connecting loop are important for incorporating the long hydrophobic alkane-like substrate. These results improve the understanding of the catalytic mechanism of CYP153D17 and provide valuable information for future protein engineering studies.
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Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding.,Lee CW, Yu SC, Lee JH, Park SH, Park H, Oh TJ, Lee JH Int J Mol Sci. 2016 Dec 9;17(12). pii: E2067. PMID:27941697<ref>PMID:27941697</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 5h1z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sphingomonas sp. pamc 26605]]
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[[Category: Sphingomonas sp. PAMC 26605]]
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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: Alkane hydroxylase]]
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[[Category: Cyp153d17]]
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[[Category: Hydrolase]]
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[[Category: P450]]
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Current revision

CYP153D17 from Sphingomonas sp. PAMC 26605

PDB ID 5h1z

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