4g8p - Revision history

OCA at 13:56, 8 November 2023

OCA — Wed, 08 Nov 2023 13:56:58 GMT

←Older revision		Revision as of 13:56, 8 November 2023
Line 1:		Line 1:

	==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==		==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
-	<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]]' scene=''>	+	<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' 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=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g8p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p ProSAT]</span></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]] 1.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Heme oxygenase (HO) catalyzes heme degradation, one of its products being carbon monoxide (CO). It is well known that CO has a higher affinity for heme iron than does molecular oxygen (O(2)); therefore, CO is potentially toxic. Because O(2) is required for the HO reaction, HO must discriminate effectively between CO and O(2) and thus escape product inhibition. Previously, we demonstrated large conformational changes in the heme-HO-1 complex upon CO binding that arise from steric hindrance between CO bound to the heme iron and Gly-139. However, we have not yet identified those changes that are specific to CO binding and do not occur upon O(2) binding. Here we determine the crystal structure of the O(2)-bound form at 1.8 A resolution and reveal the structural changes that are specific to CO binding. Moreover, difference Fourier maps comparing the structures before and after CO photolysis at <160 K clearly show structural changes such as movement of the distal F-helix upon CO photolysis. No such changes are observed upon O(2) photolysis, consistent with the structures of the ligand-free, O(2)-bound, and CO-bound forms. Protein motions even at cryogenic temperatures imply that the CO-bound heme-HO-1 complex is severely constrained (as in ligand binding to the T-state of hemoglobin), indicating that CO binding to the heme-HO-1 complex is specifically inhibited by steric hindrance. The difference Fourier maps also suggest new routes for CO migration.
		+
		+	Discrimination between CO and O(2) in heme oxygenase: comparison of static structures and dynamic conformation changes following CO photolysis.,Sugishima M, Moffat K, Noguchi M Biochemistry. 2012 Oct 30;51(43):8554-62. doi: 10.1021/bi301175x. Epub 2012 Oct, 18. PMID:23043644<ref>PMID:23043644</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]		*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Rattus norvegicus]]
	[[Category: Moffat K]]		[[Category: Moffat K]]
	[[Category: Noguchi M]]		[[Category: Noguchi M]]
	[[Category: Sugishima M]]		[[Category: Sugishima M]]

OCA at 10:42, 31 August 2022

OCA — Wed, 31 Aug 2022 10:42:35 GMT

←Older revision		Revision as of 10:42, 31 August 2022
Line 1:		Line 1:

	==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==		==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
-	<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]]~~, [[Resolution\|resolution]] 1.90Å~~' scene=''>	+	<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[4g8p]] is a 1 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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;'>[[4g7l\|4g7l]], [[4g7p\|4g7p]], [[4g7t\|4g7t]], [[4g7u\|4g7u]], [[4g8u\|4g8u]], [[4g8w\|4g8w]], [[4g98\|4g98]], [[4g99\|4g99]]</div></td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Heme oxygenase (HO) catalyzes heme degradation, one of its products being carbon monoxide (CO). It is well known that CO has a higher affinity for heme iron than does molecular oxygen (O(2)); therefore, CO is potentially toxic. Because O(2) is required for the HO reaction, HO must discriminate effectively between CO and O(2) and thus escape product inhibition. Previously, we demonstrated large conformational changes in the heme-HO-1 complex upon CO binding that arise from steric hindrance between CO bound to the heme iron and Gly-139. However, we have not yet identified those changes that are specific to CO binding and do not occur upon O(2) binding. Here we determine the crystal structure of the O(2)-bound form at 1.8 A resolution and reveal the structural changes that are specific to CO binding. Moreover, difference Fourier maps comparing the structures before and after CO photolysis at <160 K clearly show structural changes such as movement of the distal F-helix upon CO photolysis. No such changes are observed upon O(2) photolysis, consistent with the structures of the ligand-free, O(2)-bound, and CO-bound forms. Protein motions even at cryogenic temperatures imply that the CO-bound heme-HO-1 complex is severely constrained (as in ligand binding to the T-state of hemoglobin), indicating that CO binding to the heme-HO-1 complex is specifically inhibited by steric hindrance. The difference Fourier maps also suggest new routes for CO migration.
-
-	Discrimination between CO and O(2) in heme oxygenase: comparison of static structures and dynamic conformation changes following CO photolysis.,Sugishima M, Moffat K, Noguchi M Biochemistry. 2012 Oct 30;51(43):8554-62. doi: 10.1021/bi301175x. Epub 2012 Oct, 18. PMID:23043644<ref>PMID:23043644</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]		*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Heme oxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Moffat, K]]	+	[[Category: Moffat K]]
-	[[Category: Noguchi, M]]	+	[[Category: Noguchi M]]
-	[[Category: Sugishima, M]]	+	[[Category: Sugishima M]]
-	~~[[Category: All alpha protein]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxygenase~~]]	+

OCA at 05:01, 25 August 2022

OCA — Thu, 25 Aug 2022 05:01:49 GMT

←Older revision		Revision as of 05:01, 25 August 2022
Line 1:		Line 1:

	==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==		==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
-	<StructureSection load='4g8p' size='340' side='right' caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='4g8p' size='340' side='right'caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g8p]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]~~. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g8p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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">[[4g7l\|4g7l]], [[4g7p\|4g7p]], [[4g7t\|4g7t]], [[4g7u\|4g7u]], [[4g8u\|4g8u]], [[4g8w\|4g8w]], [[4g98\|4g98]], [[4g99\|4g99]]</td>~~</tr>~~	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4g7l\|4g7l]], [[4g7p\|4g7p]], [[4g7t\|4g7t]], [[4g7u\|4g7u]], [[4g8u\|4g8u]], [[4g8w\|4g8w]], [[4g98\|4g98]], [[4g99\|4g99]]</div></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])~~</td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [https://pdbe.org/4g8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [https://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [~~http~~://pdbe.org/4g8p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.	+	[[https://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Heme oxygenase 3D structures\|Heme oxygenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
		+	[[Category: Large Structures]]
	[[Category: Moffat, K]]		[[Category: Moffat, K]]
	[[Category: Noguchi, M]]		[[Category: Noguchi, M]]

OCA at 08:26, 15 November 2017

OCA — Wed, 15 Nov 2017 08:26:00 GMT

←Older revision		Revision as of 08:26, 15 November 2017
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4g8p" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Heme oxygenase\|Heme oxygenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:43, 4 August 2016

OCA — Thu, 04 Aug 2016 16:43:37 GMT

←Older revision		Revision as of 16:43, 4 August 2016
Line 1:		Line 1:
		+
	==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==		==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
	<StructureSection load='4g8p' size='340' side='right' caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='4g8p' size='340' side='right' caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://pdbe.org/4g8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4g8p" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 17:09, 24 December 2014

OCA — Wed, 24 Dec 2014 17:09:26 GMT

←Older revision		Revision as of 17:09, 24 December 2014
Line 9:		Line 9:
	<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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p 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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HMOX1_RAT HMOX1_RAT]] Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:46, 10 December 2014

OCA — Wed, 10 Dec 2014 09:46:53 GMT

←Older revision		Revision as of 09:46, 10 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4g8p.~~jpg~~\|~~left~~\|~~200px~~]]	+	==Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on==
		+	<StructureSection load='4g8p' size='340' side='right' caption='[[4g8p]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4g8p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G8P FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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">[[4g7l\|4g7l]], [[4g7p\|4g7p]], [[4g7t\|4g7t]], [[4g7u\|4g7u]], [[4g8u\|4g8u]], [[4g8w\|4g8w]], [[4g98\|4g98]], [[4g99\|4g99]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Hmox1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </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=4g8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g8p RCSB], [http://www.ebi.ac.uk/pdbsum/4g8p PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Heme oxygenase (HO) catalyzes heme degradation, one of its products being carbon monoxide (CO). It is well known that CO has a higher affinity for heme iron than does molecular oxygen (O(2)); therefore, CO is potentially toxic. Because O(2) is required for the HO reaction, HO must discriminate effectively between CO and O(2) and thus escape product inhibition. Previously, we demonstrated large conformational changes in the heme-HO-1 complex upon CO binding that arise from steric hindrance between CO bound to the heme iron and Gly-139. However, we have not yet identified those changes that are specific to CO binding and do not occur upon O(2) binding. Here we determine the crystal structure of the O(2)-bound form at 1.8 A resolution and reveal the structural changes that are specific to CO binding. Moreover, difference Fourier maps comparing the structures before and after CO photolysis at <160 K clearly show structural changes such as movement of the distal F-helix upon CO photolysis. No such changes are observed upon O(2) photolysis, consistent with the structures of the ligand-free, O(2)-bound, and CO-bound forms. Protein motions even at cryogenic temperatures imply that the CO-bound heme-HO-1 complex is severely constrained (as in ligand binding to the T-state of hemoglobin), indicating that CO binding to the heme-HO-1 complex is specifically inhibited by steric hindrance. The difference Fourier maps also suggest new routes for CO migration.

-	~~{{STRUCTURE_4g8p\| PDB=4g8p \| SCENE= }}~~	+	Discrimination between CO and O(2) in heme oxygenase: comparison of static structures and dynamic conformation changes following CO photolysis.,Sugishima M, Moffat K, Noguchi M Biochemistry. 2012 Oct 30;51(43):8554-62. doi: 10.1021/bi301175x. Epub 2012 Oct, 18. PMID:23043644<ref>PMID:23043644</ref>

-	~~===Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23043644}}~~	+	==See Also==
-		+	*[[Heme oxygenase\|Heme oxygenase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4g8p~~]] ~~is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from~~ [~~http~~:~~//oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA~~].	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Heme oxygenase]]		[[Category: Heme oxygenase]]
-	~~[[Category: Rattus norvegicus]]~~	+	[[Category: Moffat, K]]
-	[[Category: Moffat, K.]]	+	[[Category: Noguchi, M]]
-	[[Category: Noguchi, M.]]	+	[[Category: Sugishima, M]]
-	[[Category: Sugishima, M.]]	+
	[[Category: All alpha protein]]		[[Category: All alpha protein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Oxygenase]]		[[Category: Oxygenase]]

OCA at 09:05, 31 October 2012

OCA — Wed, 31 Oct 2012 09:05:45 GMT

←Older revision		Revision as of 09:05, 31 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4g8p.jpg\|left\|200px]]

-	~~The entry~~ 4g8p ~~is ON HOLD~~	+	{{STRUCTURE_4g8p\| PDB=4g8p \| SCENE= }}

-	~~Authors~~: ~~Sugishima, M., Moffat, K., Noguchi, M.~~	+	===Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on===

-	~~Description: Rat Heme Oxygenase-~~1 ~~in complex~~ with Heme ~~and CO with 16 hr Illumination~~: ~~Laser on~~	+	{{ABSTRACT_PUBMED_23043644}}
		+
		+	==About this Structure==
		+	[[4g8p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G8P OCA].
		+	[[Category: Heme oxygenase]]
		+	[[Category: Rattus norvegicus]]
		+	[[Category: Moffat, K.]]
		+	[[Category: Noguchi, M.]]
		+	[[Category: Sugishima, M.]]
		+	[[Category: All alpha protein]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxygenase]]

OCA: Protected "4g8p" [edit=sysop:move=sysop]

OCA — Wed, 01 Aug 2012 05:30:56 GMT

Protected "4g8p" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:30, 1 August 2012

OCA: New page: '''Unreleased structure''' The entry 4g8p is ON HOLD Authors: Sugishima, M., Moffat, K., Noguchi, M. Description: Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illuminati...

OCA — Wed, 01 Aug 2012 05:30:55 GMT

New page: '''Unreleased structure''' The entry 4g8p is ON HOLD Authors: Sugishima, M., Moffat, K., Noguchi, M. Description: Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illuminati...

New page

'''Unreleased structure'''

The entry 4g8p is ON HOLD

Authors: Sugishima, M., Moffat, K., Noguchi, M.

Description: Rat Heme Oxygenase-1 in complex with Heme and CO with 16 hr Illumination: Laser on