6i7g - Revision history

OCA at 11:48, 24 January 2024

2024-01-24T11:48:30Z

←Older revision		Revision as of 11:48, 24 January 2024
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	<StructureSection load='6i7g' size='340' side='right'caption='[[6i7g]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='6i7g' size='340' side='right'caption='[[6i7g]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6i7g]] 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=6I7G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6I7G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6i7g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I7G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I7G FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 2.7Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FICD, HIP13, HYPE, UNQ3041/PRO9857 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=6i7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i7g OCA], [~~http~~://pdbe.org/6i7g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6i7g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6i7g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6i7g 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=6i7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i7g OCA], [https://pdbe.org/6i7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i7g RCSB], [https://www.ebi.ac.uk/pdbsum/6i7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i7g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FICD_HUMAN FICD_HUMAN]] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.<ref>PMID:19362538</ref> <ref>PMID:22266942</ref>	+	[https://www.uniprot.org/uniprot/FICD_HUMAN FICD_HUMAN] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.<ref>PMID:19362538</ref> <ref>PMID:22266942</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Perera~~, L A~~]]	+	[[Category: Perera LA]]
-	[[Category: Read~~, R J~~]]	+	[[Category: Read RJ]]
-	[[Category: Ron, D]]	+	[[Category: Ron D]]
-	[[Category: Yan, Y]]	+	[[Category: Yan Y]]
-	~~[[Category: Ampylation]]~~	+
-	~~[[Category: Bip]]~~	+
-	~~[[Category: Fic]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Upr~~]]	+

OCA at 11:06, 2 October 2019

2019-10-02T11:06:40Z

←Older revision		Revision as of 11:06, 2 October 2019
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-	'''Unreleased structure'''

-	~~The entry~~ 6i7g is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of dimeric wild type FICD complexed with ATP==
		+	<StructureSection load='6i7g' size='340' side='right'caption='[[6i7g]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6i7g]] 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=6I7G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I7G FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FICD, HIP13, HYPE, UNQ3041/PRO9857 ([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=6i7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i7g OCA], [http://pdbe.org/6i7g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i7g RCSB], [http://www.ebi.ac.uk/pdbsum/6i7g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i7g ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FICD_HUMAN FICD_HUMAN]] Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. Able to inactivate Rho GTPases in vitro by adding AMP to RhoA, Rac and Cdc42. It is however unclear whether it inactivates GTPases in vivo and physiological substrates probably remain to be identified.<ref>PMID:19362538</ref> <ref>PMID:22266942</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	AMPylation is an inactivating modification that alters the activity of the major endoplasmic reticulum (ER) chaperone BiP to match the burden of unfolded proteins. A single ER-localised Fic protein, FICD (HYPE), catalyses both AMPylation and deAMPylation of BiP. However, the basis for the switch in FICD's activity is unknown. We report on the transition of FICD from a dimeric enzyme, that deAMPylates BiP, to a monomer with potent AMPylation activity. Mutations in the dimer interface, or of residues along an inhibitory pathway linking the dimer interface to the enzyme's active site, favour BiP AMPylation in vitro and in cells. Mechanistically, monomerisation relieves a repressive effect allosterically propagated from the dimer interface to the inhibitory Glu234, thereby permitting AMPylation-competent binding of MgATP. Moreover, a reciprocal signal, propagated from the nucleotide-binding site, provides a mechanism for coupling the oligomeric state and enzymatic activity of FICD to the energy status of the ER.

-	~~Authors~~:	+	An oligomeric state-dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP.,Perera LA, Rato C, Yan Y, Neidhardt L, McLaughlin SH, Read RJ, Preissler S, Ron D EMBO J. 2019 Sep 18:e102177. doi: 10.15252/embj.2019102177. PMID:31531998<ref>PMID:31531998</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6i7g" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
		+	[[Category: Perera, L A]]
		+	[[Category: Read, R J]]
		+	[[Category: Ron, D]]
		+	[[Category: Yan, Y]]
		+	[[Category: Ampylation]]
		+	[[Category: Bip]]
		+	[[Category: Fic]]
		+	[[Category: Transferase]]
		+	[[Category: Upr]]

OCA at 06:34, 26 December 2018

2018-12-26T06:34:13Z

←Older revision		Revision as of 06:34, 26 December 2018
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6i7g is ON HOLD	+	The entry 6i7g is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6i7g" [edit=sysop:move=sysop]

2018-12-02T18:41:34Z

Protected "6i7g" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:41, 2 December 2018

OCA: New page: '''Unreleased structure''' The entry 6i7g is ON HOLD Authors: Description: Category: Unreleased Structures

2018-12-02T18:41:32Z

New page: '''Unreleased structure''' The entry 6i7g is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6i7g is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]