5gxg - Revision history

OCA at 11:45, 2 August 2023

OCA — Wed, 02 Aug 2023 11:45:30 GMT

←Older revision		Revision as of 11:45, 2 August 2023
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	<StructureSection load='5gxg' size='340' side='right'caption='[[5gxg]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='5gxg' size='340' side='right'caption='[[5gxg]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5gxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5GXG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5gxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GXG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.7Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxg OCA], [~~http~~://pdbe.org/5gxg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5gxg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5gxg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxg 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=5gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxg OCA], [https://pdbe.org/5gxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gxg RCSB], [https://www.ebi.ac.uk/pdbsum/5gxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxg 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 22:
	==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]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Camphor 5-monooxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Hiruma, Y~~]]	+	[[Category: Pseudomonas putida]]
-	[[Category: ~~Kikui,~~ Y]]	+	[[Category: Hiruma Y]]
-	[[Category: ~~Nojiri, M~~]]	+	[[Category: Kikui Y]]
-	[[Category: ~~Ubbink,~~ M]]	+	[[Category: Nojiri M]]
-	[[Category: ~~Inter-protein electron transfer]]~~	+	[[Category: Ubbink M]]
-	~~[[Category: Oxidoreductase-electron transport complex~~]]	+

OCA at 06:45, 20 May 2020

OCA — Wed, 20 May 2020 06:45:30 GMT

←Older revision		Revision as of 06:45, 20 May 2020
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	==High-resolution crystal structure of the electron transfer complex of cytochrome p450cam with putidaredoxin==		==High-resolution crystal structure of the electron transfer complex of cytochrome p450cam with putidaredoxin==
-	<StructureSection load='5gxg' size='340' side='right' caption='[[5gxg]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='5gxg' size='340' side='right'caption='[[5gxg]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5gxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5GXG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5gxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GXG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxg OCA], [http://pdbe.org/5gxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gxg RCSB], [http://www.ebi.ac.uk/pdbsum/5gxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxg ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxg OCA], [http://pdbe.org/5gxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gxg RCSB], [http://www.ebi.ac.uk/pdbsum/5gxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5gxg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5gxg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cytochrome P450 3D structures\|Cytochrome P450 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Camphor 5-monooxygenase]]		[[Category: Camphor 5-monooxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Hiruma, Y]]		[[Category: Hiruma, Y]]
	[[Category: Kikui, Y]]		[[Category: Kikui, Y]]

OCA at 07:08, 18 October 2017

OCA — Wed, 18 Oct 2017 07:08:27 GMT

←Older revision		Revision as of 07:08, 18 October 2017
Line 10:		Line 10:
	== 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.		[[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 ==
		+	Well-defined, stereospecific states in protein complexes are often in exchange with an ensemble of more dynamic orientations: the encounter states. The structure of the stereospecific complex between cytochrome P450cam and putidaredoxin was solved recently by X-ray diffraction as well as paramagnetic NMR spectroscopy. Other than the stereospecific complex, the NMR data clearly show the presence of additional states in the complex in solution. In these encounter states, populated for a small percentage of the time, putidaredoxin assumes multiple orientations and samples a large part of the surface of cytochrome P450cam. To characterize the nature of the encounter states, an extensive paramagnetic NMR dataset has been analyzed using the Maximum Occurrence of Regions methodology. The analysis reveals the location and maximal spatial extent of the additional states needed to fully explain the NMR data. Under the assumption of sparsity of the size of the conformational ensemble, several minor states can be located quite precisely. The distribution of these minor states correlates with the electrostatic potential map around cytochrome P450cam. Whereas some minor states are on isolated positively charged patches, others are connected to the stereospecific site via positively charged paths. The existence of electrostatically favorable pathways between the stereospecific interaction site and the different minor states or lack thereof suggests a means to discriminate between productive and futile encounter states.
		+
		+	Identification of productive and futile encounters in an electron transfer protein complex.,Andralojc W, Hiruma Y, Liu WM, Ravera E, Nojiri M, Parigi G, Luchinat C, Ubbink M Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1840-E1847. doi:, 10.1073/pnas.1616813114. Epub 2017 Feb 21. PMID:28223532<ref>PMID:28223532</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5gxg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 00:39, 19 January 2017

OCA — Thu, 19 Jan 2017 00:39:10 GMT

←Older revision		Revision as of 00:39, 19 January 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5gxg is ~~ON HOLD until Paper Publication~~	+	==High-resolution crystal structure of the electron transfer complex of cytochrome p450cam with putidaredoxin==
-		+	<StructureSection load='5gxg' size='340' side='right' caption='[[5gxg]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5gxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GXG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GXG FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<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=5gxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gxg OCA], [http://pdbe.org/5gxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gxg RCSB], [http://www.ebi.ac.uk/pdbsum/5gxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gxg ProSAT]</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.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Camphor 5-monooxygenase]]
		+	[[Category: Hiruma, Y]]
		+	[[Category: Kikui, Y]]
		+	[[Category: Nojiri, M]]
		+	[[Category: Ubbink, M]]
		+	[[Category: Inter-protein electron transfer]]
		+	[[Category: Oxidoreductase-electron transport complex]]

OCA at 11:53, 19 October 2016

OCA — Wed, 19 Oct 2016 11:53:14 GMT

←Older revision		Revision as of 11:53, 19 October 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5gxg is ON HOLD	+	The entry 5gxg is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5gxg" [edit=sysop:move=sysop]

OCA — Mon, 03 Oct 2016 11:32:17 GMT

Protected "5gxg" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:32, 3 October 2016

OCA: New page: '''Unreleased structure''' The entry 5gxg is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Mon, 03 Oct 2016 11:32:16 GMT

New page: '''Unreleased structure''' The entry 5gxg is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5gxg is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]