5z9j: Difference between revisions

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== Structural highlights ==

<table><tr><td colspan='2'>~~[[5z9j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_himastatinicus_ATCC_53653 Streptomyces himastatinicus ATCC 53653].~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z9J FirstGlance]. <br>

<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z9J FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr>

<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=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=5z9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z9j OCA], [https://pdbe.org/5z9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z9j RCSB], [https://www.ebi.ac.uk/pdbsum/5z9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z9j ProSAT]</span></td></tr>

</table>

== ~~Function~~ ==

~~[https~~://~~www~~.~~uniprot~~.~~org~~/~~uniprot~~/~~G0LWB2_9ACTN G0LWB2_9ACTN]~~

== Publication Abstract from PubMed ==

Like a vast number of enzymes in nature, bacterial cytochrome P450 monooxygenases require an activated form of flavin as a cofactor for catalytic activity. Riboflavin is the precursor of FAD and FMN that serves as indispensable cofactor for flavoenzymes. In contrast to previous notions, herein we describe the identification of an electron-transfer process that is directly mediated by riboflavin for N-dealkylation by bacterial P450 monooxygenases. The electron relay from NADPH to riboflavin and then via activated oxygen to heme was proposed based on a combination of X-ray crystallography, molecular modeling and molecular dynamics simulation, site-directed mutagenesis and biochemical analysis of representative bacterial P450 monooxygenases. This study provides new insights into the electron transfer mechanism in bacterial P450 enzyme catalysis and likely in yeasts, fungi, plants and mammals.

Riboflavin Is Directly Involved in N-Dealkylation Catalyzed by Bacterial Cytochrome P450 Monooxygenases.,Zhang C, Lu M, Lin L, Huang Z, Zhang R, Wu X, Chen Y Chembiochem. 2020 Apr 3. doi: 10.1002/cbic.202000071. PMID:32243060<ref>PMID:32243060</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

~~[[Category: Streptomyces himastatinicus ATCC 53653]]~~

[[Category: Chen Y]]

[[Category: Lin L]]

[[Category: Lu M]]

[[Category: Zhang C]]

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@@ Line 3: / Line 3: @@
 <StructureSection load='5z9j' size='340' side='right'caption='[[5z9j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5z9j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_himastatinicus_ATCC_53653 Streptomyces himastatinicus ATCC 53653]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z9J FirstGlance]. <br>
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z9J FirstGlance]. <br>
 </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&#8491;</td></tr>
 <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=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=5z9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z9j OCA], [https://pdbe.org/5z9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z9j RCSB], [https://www.ebi.ac.uk/pdbsum/5z9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z9j ProSAT]</span></td></tr>
 </table>
-== Function ==
+<div style="background-color:#fffaf0;">
-[https://www.uniprot.org/uniprot/G0LWB2_9ACTN G0LWB2_9ACTN]
+== Publication Abstract from PubMed ==
+Like a vast number of enzymes in nature, bacterial cytochrome P450 monooxygenases require an activated form of flavin as a cofactor for catalytic activity. Riboflavin is the precursor of FAD and FMN that serves as indispensable cofactor for flavoenzymes. In contrast to previous notions, herein we describe the identification of an electron-transfer process that is directly mediated by riboflavin for N-dealkylation by bacterial P450 monooxygenases. The electron relay from NADPH to riboflavin and then via activated oxygen to heme was proposed based on a combination of X-ray crystallography, molecular modeling and molecular dynamics simulation, site-directed mutagenesis and biochemical analysis of representative bacterial P450 monooxygenases. This study provides new insights into the electron transfer mechanism in bacterial P450 enzyme catalysis and likely in yeasts, fungi, plants and mammals.
+Riboflavin Is Directly Involved in N-Dealkylation Catalyzed by Bacterial Cytochrome P450 Monooxygenases.,Zhang C, Lu M, Lin L, Huang Z, Zhang R, Wu X, Chen Y Chembiochem. 2020 Apr 3. doi: 10.1002/cbic.202000071. PMID:32243060<ref>PMID:32243060</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5z9j" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Streptomyces himastatinicus ATCC 53653]]
 [[Category: Chen Y]]
 [[Category: Lin L]]
 [[Category: Lu M]]
 [[Category: Zhang C]]