7qpa - Revision history

OCA at 06:24, 8 September 2022

OCA — Thu, 08 Sep 2022 06:24:32 GMT

←Older revision		Revision as of 06:24, 8 September 2022
Line 3:		Line 3:
	<StructureSection load='7qpa' size='340' side='right'caption='[[7qpa]], [[Resolution\|resolution]] 3.18Å' scene=''>		<StructureSection load='7qpa' size='340' side='right'caption='[[7qpa]], [[Resolution\|resolution]] 3.18Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7qpa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7qpa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPA FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLP:1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>DLP</scene>, <scene name='pdbligand=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLP:1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>DLP</scene>, <scene name='pdbligand=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</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;'>[[7qp9\|7qp9]], [[7qpc\|7qpc]]</div></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=7qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpa OCA], [https://pdbe.org/7qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpa RCSB], [https://www.ebi.ac.uk/pdbsum/7qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpa 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=7qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpa OCA], [https://pdbe.org/7qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpa RCSB], [https://www.ebi.ac.uk/pdbsum/7qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PIN8_ARATH PIN8_ARATH]] Component of the intracellular auxin-transport pathway in the male gametophyte (PubMed:20439545, PubMed:22540348). Involved in the regulation of auxin homeostasis in pollen (PubMed:22540348). Involved in the efflux of auxin from the endoplasmic reticulum into the cytoplasm (PubMed:22760640). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in the control of vein patterning (PubMed:23437008, PubMed:24304505). Redundantly with PIN6, inhibits the vein-formation-promoting functions of PIN5 (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462).<ref>PMID:20439545</ref> <ref>PMID:22540348</ref> <ref>PMID:22760640</ref> <ref>PMID:23437008</ref> <ref>PMID:24304505</ref> <ref>PMID:26560462</ref> <ref>PMID:22990451</ref>	+	[[https://www.uniprot.org/uniprot/PIN8_ARATH PIN8_ARATH]] Component of the intracellular auxin-transport pathway in the male gametophyte (PubMed:20439545, PubMed:22540348). Involved in the regulation of auxin homeostasis in pollen (PubMed:22540348). Involved in the efflux of auxin from the endoplasmic reticulum into the cytoplasm (PubMed:22760640). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in the control of vein patterning (PubMed:23437008, PubMed:24304505). Redundantly with PIN6, inhibits the vein-formation-promoting functions of PIN5 (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462).<ref>PMID:20439545</ref> <ref>PMID:22540348</ref> <ref>PMID:22760640</ref> <ref>PMID:23437008</ref> <ref>PMID:24304505</ref> <ref>PMID:26560462</ref> <ref>PMID:22990451</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants(1-3). The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space(4-9). Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development.	+
-		+
-	Structures and mechanism of the plant PIN-FORMED auxin transporter.,Ung KL, Winkler M, Schulz L, Kolb M, Janacek DP, Dedic E, Stokes DL, Hammes UZ, Pedersen BP Nature. 2022 Jun 29. pii: 10.1038/s41586-022-04883-y. doi:, 10.1038/s41586-022-04883-y. PMID:35768502<ref>PMID:35768502</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7qpa" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Arabidopsis thaliana]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dedic, E]]	+	[[Category: Dedic E]]
-	[[Category: Pedersen~~, B P~~]]	+	[[Category: Pedersen BP]]
-	[[Category: Stokes~~, D L~~]]	+	[[Category: Stokes DL]]
-	[[Category: Ung~~, K L~~]]	+	[[Category: Ung KL]]
-	[[Category: Winkler~~, M B.L]]~~	+	[[Category: Winkler MBL]]
-	~~[[Category: Aec family]]~~	+
-	~~[[Category: Auxin transport]]~~	+
-	~~[[Category: Bart superfamily]]~~	+
-	~~[[Category: Membrane protein~~]]	+

OCA at 05:25, 13 July 2022

OCA — Wed, 13 Jul 2022 05:25:32 GMT

←Older revision		Revision as of 05:25, 13 July 2022
Line 1:		Line 1:

	==Outward-facing auxin bound form of auxin transporter PIN8==		==Outward-facing auxin bound form of auxin transporter PIN8==
-	<StructureSection load='7qpa' size='340' side='right'caption='[[7qpa]]' scene=''>	+	<StructureSection load='7qpa' size='340' side='right'caption='[[7qpa]], [[Resolution\|resolution]] 3.18Å' 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=7QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7qpa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPA 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=7qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpa OCA], [https://pdbe.org/7qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpa RCSB], [https://www.ebi.ac.uk/pdbsum/7qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpa ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLP:1,2-DILINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>DLP</scene>, <scene name='pdbligand=IAC:1H-INDOL-3-YLACETIC+ACID'>IAC</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;'>[[7qp9\|7qp9]], [[7qpc\|7qpc]]</div></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=7qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpa OCA], [https://pdbe.org/7qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpa RCSB], [https://www.ebi.ac.uk/pdbsum/7qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpa ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/PIN8_ARATH PIN8_ARATH]] Component of the intracellular auxin-transport pathway in the male gametophyte (PubMed:20439545, PubMed:22540348). Involved in the regulation of auxin homeostasis in pollen (PubMed:22540348). Involved in the efflux of auxin from the endoplasmic reticulum into the cytoplasm (PubMed:22760640). PIN5 and PIN8 may have an antagonistic/compensatory activity (PubMed:22760640, PubMed:22990451). Involved in the control of vein patterning (PubMed:23437008, PubMed:24304505). Redundantly with PIN6, inhibits the vein-formation-promoting functions of PIN5 (PubMed:26560462). PIN5, PIN6, and PIN8 control vein network geometry, but they are expressed in mutually exclusive domains of leaf vascular cells (PubMed:26560462).<ref>PMID:20439545</ref> <ref>PMID:22540348</ref> <ref>PMID:22760640</ref> <ref>PMID:23437008</ref> <ref>PMID:24304505</ref> <ref>PMID:26560462</ref> <ref>PMID:22990451</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Auxins are hormones that have central roles and control nearly all aspects of growth and development in plants(1-3). The proteins in the PIN-FORMED (PIN) family (also known as the auxin efflux carrier family) are key participants in this process and control auxin export from the cytosol to the extracellular space(4-9). Owing to a lack of structural and biochemical data, the molecular mechanism of PIN-mediated auxin transport is not understood. Here we present biophysical analysis together with three structures of Arabidopsis thaliana PIN8: two outward-facing conformations with and without auxin, and one inward-facing conformation bound to the herbicide naphthylphthalamic acid. The structure forms a homodimer, with each monomer divided into a transport and scaffold domain with a clearly defined auxin binding site. Next to the binding site, a proline-proline crossover is a pivot point for structural changes associated with transport, which we show to be independent of proton and ion gradients and probably driven by the negative charge of the auxin. The structures and biochemical data reveal an elevator-type transport mechanism reminiscent of bile acid/sodium symporters, bicarbonate/sodium symporters and sodium/proton antiporters. Our results provide a comprehensive molecular model for auxin recognition and transport by PINs, link and expand on a well-known conceptual framework for transport, and explain a central mechanism of polar auxin transport, a core feature of plant physiology, growth and development.
		+
		+	Structures and mechanism of the plant PIN-FORMED auxin transporter.,Ung KL, Winkler M, Schulz L, Kolb M, Janacek DP, Dedic E, Stokes DL, Hammes UZ, Pedersen BP Nature. 2022 Jun 29. pii: 10.1038/s41586-022-04883-y. doi:, 10.1038/s41586-022-04883-y. PMID:35768502<ref>PMID:35768502</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7qpa" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dedic E]]	+	[[Category: Dedic, E]]
-	[[Category: Pedersen BP]]	+	[[Category: Pedersen, B P]]
-	[[Category: Stokes DL]]	+	[[Category: Stokes, D L]]
-	[[Category: Ung KL]]	+	[[Category: Ung, K L]]
-	[[Category: Winkler ~~MBL~~]]	+	[[Category: Winkler, M B.L]]
		+	[[Category: Aec family]]
		+	[[Category: Auxin transport]]
		+	[[Category: Bart superfamily]]
		+	[[Category: Membrane protein]]

OCA at 16:12, 6 July 2022

OCA — Wed, 06 Jul 2022 16:12:54 GMT

←Older revision		Revision as of 16:12, 6 July 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7qpa is ~~ON HOLD until Paper Publication~~	+	==Outward-facing auxin bound form of auxin transporter PIN8==
-		+	<StructureSection load='7qpa' size='340' side='right'caption='[[7qpa]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPA FirstGlance]. <br>
-	~~Description~~:	+	</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=7qpa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpa OCA], [https://pdbe.org/7qpa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpa RCSB], [https://www.ebi.ac.uk/pdbsum/7qpa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpa ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Dedic E]]
		+	[[Category: Pedersen BP]]
		+	[[Category: Stokes DL]]
		+	[[Category: Ung KL]]
		+	[[Category: Winkler MBL]]

OCA at 05:17, 27 January 2022

OCA — Thu, 27 Jan 2022 05:17:42 GMT

←Older revision		Revision as of 05:17, 27 January 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7qpa is ON HOLD	+	The entry 7qpa is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "7qpa" [edit=sysop:move=sysop]

OCA — Wed, 12 Jan 2022 08:30:46 GMT

Protected "7qpa" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:30, 12 January 2022

OCA: New page: '''Unreleased structure''' The entry 7qpa is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 12 Jan 2022 08:30:45 GMT

New page: '''Unreleased structure''' The entry 7qpa is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7qpa is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]