5e78
From Proteopedia
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<StructureSection load='5e78' size='340' side='right' caption='[[5e78]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='5e78' size='340' side='right' caption='[[5e78]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5e78]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E78 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5e78]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E78 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5KK:1,3,6,8,10,13,16,19-OCTAAZABICYCLO[6.6.6]ICOSANE'>5KK</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5KK:1,3,6,8,10,13,16,19-OCTAAZABICYCLO[6.6.6]ICOSANE'>5KK</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e78 OCA], [http://pdbe.org/5e78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e78 RCSB], [http://www.ebi.ac.uk/pdbsum/5e78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e78 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5e78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e78 OCA], [http://pdbe.org/5e78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e78 RCSB], [http://www.ebi.ac.uk/pdbsum/5e78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e78 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450. | [[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | P450 BM3 is a multi-domain heme-containing soluble bacterial monooxygenase. P450 BM3 and variants are known to oxidize structurally diverse substrates. Crystal structures of individual domains of P450 BM3 are available. However, the spatial organization of the full-length protein is unknown. In this study, crystal structures of the P450 BM3 M7 heme domain variant with and without cobalt (III) sepulchrate are reported. Cobalt (III) sepulchrate acts as an electron shuttle in an alternative cofactor system employing zinc dust as the electron source. The crystal structure shows a binding site for the mediator cobalt (III) sepulchrate at the entrance of the substrate access channel. The mediator occupies an unusual position which is far from the active site and distinct from the binding of the natural redox partner (FAD/NADPH binding domain). | ||
| + | |||
| + | Crystallographic insights into a cobalt (III) sepulchrate based alternative cofactor system of P450 BM3 monooxygenase.,Panneerselvam S, Shehzad A, Mueller-Dieckmann J, Wilmanns M, Bocola M, Davari MD, Schwaneberg U Biochim Biophys Acta. 2018 Jan;1866(1):134-140. doi:, 10.1016/j.bbapap.2017.07.010. Epub 2017 Jul 22. PMID:28739446<ref>PMID:28739446</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5e78" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 14581]] | ||
[[Category: Bocola, M]] | [[Category: Bocola, M]] | ||
[[Category: Mueller-Dieckmann, J]] | [[Category: Mueller-Dieckmann, J]] | ||
Revision as of 09:54, 22 November 2017
Crystal structure of P450 BM3 heme domain variant complexed with Co(III)Sep
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