2m56 - Revision history

OCA at 05:59, 15 May 2024

OCA — Wed, 15 May 2024 05:59:53 GMT

←Older revision		Revision as of 05:59, 15 May 2024
Line 3:		Line 3:
	<StructureSection load='2m56' size='340' side='right'caption='[[2m56]]' scene=''>		<StructureSection load='2m56' size='340' side='right'caption='[[2m56]]' 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=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
-	</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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU] Involved in a camphor oxidation system.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cytochrome P450cam catalyzes the hydroxylation of camphor in a complex process involving two electron transfers (ETs) from the iron-sulfur protein putidaredoxin. The enzymatic control of the successive steps of catalysis is critical for a highly efficient reaction. The injection of the successive electrons is part of the control system. To understand the molecular interactions between putidaredoxin and cytochrome P450cam, we determined the structure of the complex both in solution and in the crystal state. Paramagnetic NMR spectroscopy using lanthanide tags yielded 446 structural restraints that were used to determine the solution structure. An ensemble of 10 structures with an RMSD of 1.3A was obtained. The crystal structure of the complex was solved, showing a position of putidaredoxin that is identical with the one in the solution structure. The NMR data further demonstrate the presence of a minor state or set of states of the complex in solution, which is attributed to the presence of an encounter complex. The structure of the major state shows a small binding interface and a metal-to-metal distance of 16A, with two pathways that provide strong electronic coupling of the redox centers. The interpretation of these results is discussed in the context of ET. The structure indicates that the ET rate can be much faster than the reported value, suggesting that the process may be gated.
		+
		+	The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.,Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, Lohr F, Schwalbe H, Nojiri M, Ubbink M J Mol Biol. 2013 Jul 13. pii: S0022-2836(13)00438-5. doi:, 10.1016/j.jmb.2013.07.006. PMID:23856620<ref>PMID:23856620</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 2m56" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]		*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]		*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Pseudomonas putida]]
	[[Category: Hass MAS]]		[[Category: Hass MAS]]
	[[Category: Hiruma Y]]		[[Category: Hiruma Y]]
	[[Category: Ubbink M]]		[[Category: Ubbink M]]

OCA at 10:19, 31 August 2022

OCA — Wed, 31 Aug 2022 10:19:08 GMT

←Older revision		Revision as of 10:19, 31 August 2022
Line 1:		Line 1:

	==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==		==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==
-	<StructureSection load='2m56' size='340' side='right'caption='[[2m56~~]], [[NMR_Ensembles_of_Models \| 10 NMR models~~]]' scene=''>	+	<StructureSection load='2m56' size='340' side='right'caption='[[2m56]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[2m56]] is a 2 chain structure.~~ Full ~~experimental~~ information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>	+	</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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dz4\|1dz4]], [[1xlp\|1xlp]]</div></td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[https://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Cytochrome P450cam catalyzes the hydroxylation of camphor in a complex process involving two electron transfers (ETs) from the iron-sulfur protein putidaredoxin. The enzymatic control of the successive steps of catalysis is critical for a highly efficient reaction. The injection of the successive electrons is part of the control system. To understand the molecular interactions between putidaredoxin and cytochrome P450cam, we determined the structure of the complex both in solution and in the crystal state. Paramagnetic NMR spectroscopy using lanthanide tags yielded 446 structural restraints that were used to determine the solution structure. An ensemble of 10 structures with an RMSD of 1.3A was obtained. The crystal structure of the complex was solved, showing a position of putidaredoxin that is identical with the one in the solution structure. The NMR data further demonstrate the presence of a minor state or set of states of the complex in solution, which is attributed to the presence of an encounter complex. The structure of the major state shows a small binding interface and a metal-to-metal distance of 16A, with two pathways that provide strong electronic coupling of the redox centers. The interpretation of these results is discussed in the context of ET. The structure indicates that the ET rate can be much faster than the reported value, suggesting that the process may be gated.
-
-	The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.,Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, Lohr F, Schwalbe H, Nojiri M, Ubbink M J Mol Biol. 2013 Jul 13. pii: S0022-2836(13)00438-5. doi:, 10.1016/j.jmb.2013.07.006. PMID:23856620<ref>PMID:23856620</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2m56" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]		*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]		*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Camphor 5-monooxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hass~~, M A.S~~]]	+	[[Category: Hass MAS]]
-	[[Category: Hiruma, Y]]	+	[[Category: Hiruma Y]]
-	[[Category: Ubbink, M]]	+	[[Category: Ubbink M]]
-	~~[[Category: Camphor]]~~	+
-	~~[[Category: Electron transfer]]~~	+
-	~~[[Category: Ferredoxin]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Iron-sulphor]]~~	+
-	~~[[Category: Lanthanide]]~~	+
-	~~[[Category: Oxidoreductase-metal binding protein complex]]~~	+
-	~~[[Category: Paramagnetic~~]]	+

OCA at 04:53, 25 August 2022

OCA — Thu, 25 Aug 2022 04:53:50 GMT

←Older revision		Revision as of 04:53, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='2m56' size='340' side='right'caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2m56' size='340' side='right'caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure ~~with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dz4\|1dz4]], [[1xlp\|1xlp]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dz4\|1dz4]], [[1xlp\|1xlp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>
Line 29:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 10:59, 19 May 2021

OCA — Wed, 19 May 2021 10:59:47 GMT

←Older revision		Revision as of 10:59, 19 May 2021
Line 1:		Line 1:

	==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==		==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==
-	<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>	+	<StructureSection load='2m56' size='340' side='right'caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2M56 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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" id="ligandDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dz4\|1dz4]], [[1xlp\|1xlp]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dz4\|1dz4]], [[1xlp\|1xlp]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [~~http~~://pdbe.org/2m56 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [https://pdbe.org/2m56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [https://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[~~http~~://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.	+	[[https://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[https://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Cytochrome P450\|Cytochrome P450]]	+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
-	*[[Ferredoxin\|Ferredoxin]]	+	*[[Ferredoxin 3D structures\|Ferredoxin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 31:		Line 31:
	[[Category: Bacillus fluorescens putidus flugge 1886]]		[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Hass, M A.S]]		[[Category: Hass, M A.S]]
	[[Category: Hiruma, Y]]		[[Category: Hiruma, Y]]

OCA at 22:31, 9 August 2018

OCA — Thu, 09 Aug 2018 22:31:10 GMT

←Older revision		Revision as of 22:31, 9 August 2018
Line 1:		Line 1:
		+
	==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==		==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==
	<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [http://pdbe.org/2m56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [http://www.ebi.ac.uk/pdbsum/2m56 PDBsum]</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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [http://pdbe.org/2m56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [http://www.ebi.ac.uk/pdbsum/2m56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2m56 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 14:16, 11 September 2015

OCA — Fri, 11 Sep 2015 14:16:24 GMT

←Older revision		Revision as of 14:16, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>		<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Pseudomonas_putida Pseudomonas putida~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M56 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dz4\|1dz4]], [[1xlp\|1xlp]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dz4\|1dz4]], [[1xlp\|1xlp]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 ~~Pseudomonas putida~~]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 ~~Pseudomonas putida~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [http://www.ebi.ac.uk/pdbsum/2m56 PDBsum]</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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [http://pdbe.org/2m56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [http://www.ebi.ac.uk/pdbsum/2m56 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2m56" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus fluorescens putidus flugge 1886]]
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
-	[[Category: Pseudomonas putida]]
	[[Category: Hass, M A.S]]		[[Category: Hass, M A.S]]
	[[Category: Hiruma, Y]]		[[Category: Hiruma, Y]]

OCA at 17:35, 25 December 2014

OCA — Thu, 25 Dec 2014 17:35:19 GMT

←Older revision		Revision as of 17:35, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2m56\| PDB=2m56 \| SCENE= }}~~	+	==The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy==
-	===The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy===	+	<StructureSection load='2m56' size='340' side='right' caption='[[2m56]], [[NMR_Ensembles_of_Models \| 10 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_23856620}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M56 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAM:CAMPHOR'>CAM</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1dz4\|1dz4]], [[1xlp\|1xlp]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">camC, cyp101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida]), camB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Camphor_5-monooxygenase Camphor 5-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.1 1.14.15.1] </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=2m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m56 RCSB], [http://www.ebi.ac.uk/pdbsum/2m56 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[http://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.		[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[http://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cytochrome P450cam catalyzes the hydroxylation of camphor in a complex process involving two electron transfers (ETs) from the iron-sulfur protein putidaredoxin. The enzymatic control of the successive steps of catalysis is critical for a highly efficient reaction. The injection of the successive electrons is part of the control system. To understand the molecular interactions between putidaredoxin and cytochrome P450cam, we determined the structure of the complex both in solution and in the crystal state. Paramagnetic NMR spectroscopy using lanthanide tags yielded 446 structural restraints that were used to determine the solution structure. An ensemble of 10 structures with an RMSD of 1.3A was obtained. The crystal structure of the complex was solved, showing a position of putidaredoxin that is identical with the one in the solution structure. The NMR data further demonstrate the presence of a minor state or set of states of the complex in solution, which is attributed to the presence of an encounter complex. The structure of the major state shows a small binding interface and a metal-to-metal distance of 16A, with two pathways that provide strong electronic coupling of the redox centers. The interpretation of these results is discussed in the context of ET. The structure indicates that the ET rate can be much faster than the reported value, suggesting that the process may be gated.
		+
		+	The Structure of the Cytochrome P450cam-Putidaredoxin Complex Determined by Paramagnetic NMR Spectroscopy and Crystallography.,Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, Lohr F, Schwalbe H, Nojiri M, Ubbink M J Mol Biol. 2013 Jul 13. pii: S0022-2836(13)00438-5. doi:, 10.1016/j.jmb.2013.07.006. PMID:23856620<ref>PMID:23856620</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[2m56]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Pseudomonas_putida Pseudomonas putida]~~. ~~Full experimental information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023856620</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Cytochrome P450\|Cytochrome P450]]
		+	*[[Ferredoxin\|Ferredoxin]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
	[[Category: Pseudomonas putida]]		[[Category: Pseudomonas putida]]
-	[[Category: Hass, M A.S.]]	+	[[Category: Hass, M A.S]]
-	[[Category: Hiruma, Y.]]	+	[[Category: Hiruma, Y]]
-	[[Category: Ubbink, M.]]	+	[[Category: Ubbink, M]]
	[[Category: Camphor]]		[[Category: Camphor]]
	[[Category: Electron transfer]]		[[Category: Electron transfer]]

OCA at 08:21, 21 August 2013

OCA — Wed, 21 Aug 2013 08:21:04 GMT

←Older revision		Revision as of 08:21, 21 August 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_2m56\| PDB=2m56 \| SCENE= }}
		+	===The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy===
		+	{{ABSTRACT_PUBMED_23856620}}

-	The ~~entry 2m56 is ON HOLD until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/CPXA_PSEPU CPXA_PSEPU]] Involved in a camphor oxidation system. [[http://www.uniprot.org/uniprot/PUTX_PSEPU PUTX_PSEPU]] The oxidation of camphor by cytochrome P450-CAM requires the participation of a flavoprotein, putidaredoxin reductase, and an iron-sulfur protein, putidaredoxin, to mediate the transfer of electrons from NADH to P450 for oxygen activation.

-	~~Authors~~: ~~Hiruma, Y~~.~~, Hass, M~~.A.S.~~, Ubbink, M~~.	+	==About this Structure==
		+	[[2m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M56 OCA].

-	~~Description~~: ~~The structure of the~~ complex ~~of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy~~	+	==Reference==
		+	<ref group="xtra">PMID:023856620</ref><references group="xtra"/><references/>
		+	[[Category: Camphor 5-monooxygenase]]
		+	[[Category: Pseudomonas putida]]
		+	[[Category: Hass, M A.S.]]
		+	[[Category: Hiruma, Y.]]
		+	[[Category: Ubbink, M.]]
		+	[[Category: Camphor]]
		+	[[Category: Electron transfer]]
		+	[[Category: Ferredoxin]]
		+	[[Category: Heme]]
		+	[[Category: Iron-sulphor]]
		+	[[Category: Lanthanide]]
		+	[[Category: Oxidoreductase-metal binding protein complex]]
		+	[[Category: Paramagnetic]]

OCA at 06:48, 14 August 2013

OCA — Wed, 14 Aug 2013 06:48:18 GMT

←Older revision		Revision as of 06:48, 14 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2m56 is ON HOLD	+	The entry 2m56 is ON HOLD until Paper Publication

	Authors: Hiruma, Y., Hass, M.A.S., Ubbink, M.		Authors: Hiruma, Y., Hass, M.A.S., Ubbink, M.

	Description: The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy		Description: The structure of the complex of cytochrome P450cam and its electron donor putidaredoxin determined by paramagnetic NMR spectroscopy

OCA: Protected "2m56" [edit=sysop:move=sysop]

OCA — Wed, 20 Feb 2013 13:07:59 GMT

Protected "2m56" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:07, 20 February 2013