6hzm - Revision history

OCA at 01:36, 11 April 2020

OCA — Sat, 11 Apr 2020 01:36:11 GMT

←Older revision		Revision as of 01:36, 11 April 2020
Line 3:		Line 3:
	<SX load='6hzm' size='340' side='right' viewer='molstar' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>		<SX load='6hzm' size='340' side='right' viewer='molstar' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6HZM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6hbu\|6hbu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6hbu\|6hbu]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ABCG2, ABCP, BCRP, BCRP1, MXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ABCG2, ABCP, BCRP, BCRP1, MXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm 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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 21:58, 6 March 2020

OCA — Fri, 06 Mar 2020 21:58:33 GMT

←Older revision		Revision as of 21:58, 6 March 2020
Line 1:		Line 1:

	==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==		==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==
-	<~~StructureSection~~ load='6hzm' size='340' side='right'caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>	+	<SX load='6hzm' size='340' side='right' viewer='molstar' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>		<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
Line 23:		Line 23:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 10:44, 18 December 2019

OCA — Wed, 18 Dec 2019 10:44:24 GMT

←Older revision		Revision as of 10:44, 18 December 2019
Line 1:		Line 1:

	==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==		==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==
-	<StructureSection load='6hzm' size='340' side='right' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>	+	<StructureSection load='6hzm' size='340' side='right'caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>		<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Jackson, S M]]		[[Category: Jackson, S M]]
	[[Category: Kowal, J]]		[[Category: Kowal, J]]

OCA at 21:08, 2 December 2018

OCA — Sun, 02 Dec 2018 21:08:26 GMT

←Older revision		Revision as of 21:08, 2 December 2018
Line 3:		Line 3:
	<StructureSection load='6hzm' size='340' side='right' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>		<StructureSection load='6hzm' size='340' side='right' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6hbu\|6hbu]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6hbu\|6hbu]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ABCG2, ABCP, BCRP, BCRP1, MXR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm 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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ABCG2_HUMAN ABCG2_HUMAN]] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.<ref>PMID:12958161</ref> <ref>PMID:20705604</ref> <ref>PMID:22132962</ref> <ref>PMID:23189181</ref>		[[http://www.uniprot.org/uniprot/ABCG2_HUMAN ABCG2_HUMAN]] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.<ref>PMID:12958161</ref> <ref>PMID:20705604</ref> <ref>PMID:22132962</ref> <ref>PMID:23189181</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	ABCG2 is a transporter protein of the ATP-binding-cassette (ABC) family that is expressed in the plasma membrane in cells of various tissues and tissue barriers, including the blood-brain, blood-testis and maternal-fetal barriers(1-4). Powered by ATP, it translocates endogenous substrates, affects the pharmacokinetics of many drugs and protects against a wide array of xenobiotics, including anti-cancer drugs(5-12). Previous studies have revealed the architecture of ABCG2 and the structural basis of its inhibition by small molecules and antibodies(13,14). However, the mechanisms of substrate recognition and ATP-driven transport are unknown. Here we present high-resolution cryo-electron microscopy (cryo-EM) structures of human ABCG2 in a substrate-bound pre-translocation state and an ATP-bound post-translocation state. For both structures, we used a mutant containing a glutamine replacing the catalytic glutamate (ABCG2EQ), which resulted in reduced ATPase and transport rates and facilitated conformational trapping for structural studies. In the substrate-bound state, a single molecule of estrone-3-sulfate (E1S) is bound in a central, hydrophobic and cytoplasm-facing cavity about halfway across the membrane. Only one molecule of E1S can bind in the observed binding mode. In the ATP-bound state, the substrate-binding cavity has collapsed while an external cavity has opened to the extracellular side of the membrane. The ATP-induced conformational changes include rigid-body shifts of the transmembrane domains, pivoting of the nucleotide-binding domains (NBDs), and a change in the relative orientation of the NBD subdomains. Mutagenesis and in vitro characterization of transport and ATPase activities demonstrate the roles of specific residues in substrate recognition, including a leucine residue that forms a 'plug' between the two cavities. Our results show how ABCG2 harnesses the energy of ATP binding to extrude E1S and other substrates, and suggest that the size and binding affinity of compounds are important for distinguishing substrates from inhibitors.
		+
		+	Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states.,Manolaridis I, Jackson SM, Taylor NMI, Kowal J, Stahlberg H, Locher KP Nature. 2018 Nov;563(7731):426-430. doi: 10.1038/s41586-018-0680-3. Epub 2018 Nov, 7. PMID:30405239<ref>PMID:30405239</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6hzm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Jackson, S M]]		[[Category: Jackson, S M]]
	[[Category: Kowal, J]]		[[Category: Kowal, J]]

OCA at 08:21, 14 November 2018

OCA — Wed, 14 Nov 2018 08:21:31 GMT

←Older revision		Revision as of 08:21, 14 November 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6hzm is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==
-		+	<StructureSection load='6hzm' size='340' side='right' caption='[[6hzm]], [[Resolution\|resolution]] 3.09Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6hbu\|6hbu]]</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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ABCG2_HUMAN ABCG2_HUMAN]] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.<ref>PMID:12958161</ref> <ref>PMID:20705604</ref> <ref>PMID:22132962</ref> <ref>PMID:23189181</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Jackson, S M]]
		+	[[Category: Kowal, J]]
		+	[[Category: Locher, K P]]
		+	[[Category: Manolaridis, I]]
		+	[[Category: Stahlberg, H]]
		+	[[Category: Taylor, N M.I]]
		+	[[Category: Cancer]]
		+	[[Category: Membrane protein]]
		+	[[Category: Multidrug transporter]]

OCA: Protected "6hzm" [edit=sysop:move=sysop]

OCA — Wed, 31 Oct 2018 05:14:19 GMT

Protected "6hzm" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:14, 31 October 2018

OCA: New page: '''Unreleased structure''' The entry 6hzm is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

OCA — Wed, 31 Oct 2018 05:14:18 GMT

New page: '''Unreleased structure''' The entry 6hzm is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6hzm is ON HOLD until Paper Publication

Authors:

Description:
[[Category: Unreleased Structures]]