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==Crystal structure of CYP116B46-N(20-445) from Tepidiphilus thermophilus in complex with HEME== | ==Crystal structure of CYP116B46-N(20-445) from Tepidiphilus thermophilus in complex with HEME== | ||
<StructureSection load='6ldl' size='340' side='right'caption='[[6ldl]]' scene=''> | <StructureSection load='6ldl' size='340' side='right'caption='[[6ldl]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LDL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ldl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tepidiphilus_thermophilus Tepidiphilus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LDL FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.38Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=6ldl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ldl OCA], [https://pdbe.org/6ldl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ldl RCSB], [https://www.ebi.ac.uk/pdbsum/6ldl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ldl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0K6ITW2_9PROT A0A0K6ITW2_9PROT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 A. The role of several residues located between the [2Fe-2S] cluster and heme in the catalytic reaction is probed in mutagenesis experiments. These findings not only provide insights into the intramolecular electron transfer of self-sufficient P450s, but are also of interest for biotechnological applications of self-sufficient P450s. | |||
Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.,Zhang L, Xie Z, Liu Z, Zhou S, Ma L, Liu W, Huang JW, Ko TP, Li X, Hu Y, Min J, Yu X, Guo RT, Chen CC Nat Commun. 2020 May 29;11(1):2676. doi: 10.1038/s41467-020-16500-5. PMID:32472090<ref>PMID:32472090</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ldl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Tepidiphilus thermophilus]] | |||
[[Category: Chen CC]] | [[Category: Chen CC]] | ||
[[Category: Guo RT]] | [[Category: Guo RT]] | ||
Latest revision as of 13:57, 22 November 2023
Crystal structure of CYP116B46-N(20-445) from Tepidiphilus thermophilus in complex with HEMECrystal structure of CYP116B46-N(20-445) from Tepidiphilus thermophilus in complex with HEME
Structural highlights
FunctionPublication Abstract from PubMedCytochrome P450 monooxygenases are versatile heme-thiolate enzymes that catalyze a wide range of reactions. Self-sufficient cytochrome P450 enzymes contain the redox partners in a single polypeptide chain. Here, we present the crystal structure of full-length CYP116B46, a self-sufficient P450. The continuous polypeptide chain comprises three functional domains, which align well with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 A. The role of several residues located between the [2Fe-2S] cluster and heme in the catalytic reaction is probed in mutagenesis experiments. These findings not only provide insights into the intramolecular electron transfer of self-sufficient P450s, but are also of interest for biotechnological applications of self-sufficient P450s. Structural insight into the electron transfer pathway of a self-sufficient P450 monooxygenase.,Zhang L, Xie Z, Liu Z, Zhou S, Ma L, Liu W, Huang JW, Ko TP, Li X, Hu Y, Min J, Yu X, Guo RT, Chen CC Nat Commun. 2020 May 29;11(1):2676. doi: 10.1038/s41467-020-16500-5. PMID:32472090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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