3shg - Revision history

OCA at 09:50, 1 March 2024

2024-03-01T09:50:40Z

←Older revision		Revision as of 09:50, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3shg' size='340' side='right'caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3shg' size='340' side='right'caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Barsr Barsr~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_R1 Bartonella schoenbuchensis R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=TLA:L(+)~~-~~TARTARIC+ACID'>TLA</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]] 1.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2jk8\|2jk8]]~~</~~div~~>~~</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR]), B11C_100027 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR])</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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [https://pdbe.org/3shg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [https://www.ebi.ac.uk/pdbsum/3shg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shg 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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [https://pdbe.org/3shg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [https://www.ebi.ac.uk/pdbsum/3shg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/VBHT_BARSR VBHT_BARSR]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[https://www.uniprot.org/uniprot/VBHA_BARSR VBHA_BARSR]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.	+	[https://www.uniprot.org/uniprot/VBHA_BARSR VBHA_BARSR] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Fic proteins that are defined by the ubiquitous FIC (filamentation induced by cyclic AMP) domain are known to catalyse adenylylation (also called AMPylation); that is, the transfer of AMP onto a target protein. In mammalian cells, adenylylation of small GTPases through Fic proteins injected by pathogenic bacteria can cause collapse of the actin cytoskeleton and cell death. It is unknown how this potentially deleterious adenylylation activity is regulated in the widespread Fic proteins that are found in all domains of life and that are thought to have critical roles in intrinsic signalling processes. Here we show that FIC-domain-mediated adenylylation is controlled by a conserved mechanism of ATP-binding-site obstruction that involves an inhibitory alpha-helix (alpha(inh)) with a conserved (S/T)XXXE(G/N) motif, and that in this mechanism the invariable glutamate competes with ATP gamma-phosphate binding. Consistent with this, FIC-domain-mediated growth arrest of bacteria by the VbhT toxin of Bartonella schoenbuchensis is intermolecularly repressed by the VbhA antitoxin through tight binding of its alpha(inh) to the FIC domain of VbhT, as shown by structure and function analysis. Furthermore, structural comparisons with other bacterial Fic proteins, such as Fic of Neisseria meningitidis and of Shewanella oneidensis, show that alpha(inh) frequently constitutes an amino-terminal or carboxy-terminal extension to the FIC domain, respectively, partially obstructing the ATP binding site in an intramolecular manner. After mutation of the inhibitory motif in various Fic proteins, including the human homologue FICD (also known as HYPE), adenylylation activity is considerably boosted, consistent with the anticipated relief of inhibition. Structural homology modelling of all annotated Fic proteins indicates that inhibition by alpha(inh) is universal and conserved through evolution, as the inhibitory motif is present in approximately 90% of all putatively adenylylation-active FIC domains, including examples from all domains of life and from viruses. Future studies should reveal how intrinsic or extrinsic factors modulate adenylylation activity by weakening the interaction of alpha(inh) with the FIC active site.	+
-		+
-	Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.,Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942<ref>PMID:22266942</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3shg" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Barsr~~]]	+	[[Category: Bartonella schoenbuchensis R1]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Goepfert, A]]	+	[[Category: Goepfert A]]
-	[[Category: Schirmer, T]]	+	[[Category: Schirmer T]]
-	~~[[Category: Adenylylation]]~~	+
-	~~[[Category: Amp transfer]]~~	+
-	~~[[Category: Ampylation]]~~	+
-	~~[[Category: Fic fold]]~~	+
-	~~[[Category: Toxin-antitoxin complex]]~~	+
-	~~[[Category: Transferase-protein binding complex~~]]	+

OCA at 07:56, 29 June 2022

2022-06-29T07:56:21Z

←Older revision		Revision as of 07:56, 29 June 2022
Line 1:		Line 1:

	==VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin==		==VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin==
-	<StructureSection load='3shg' size='340' side='right' caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='3shg' size='340' side='right'caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Barsr Barsr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3SHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Barsr Barsr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jk8\|2jk8]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR]), B11C_100027 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR]), B11C_100027 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR])</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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [~~http~~://pdbe.org/3shg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3shg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3shg 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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [https://pdbe.org/3shg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [https://www.ebi.ac.uk/pdbsum/3shg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/VBHT_BARSR VBHT_BARSR]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[~~http~~://www.uniprot.org/uniprot/VBHA_BARSR VBHA_BARSR]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.	+	[[https://www.uniprot.org/uniprot/VBHT_BARSR VBHT_BARSR]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[https://www.uniprot.org/uniprot/VBHA_BARSR VBHA_BARSR]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Barsr]]		[[Category: Barsr]]
		+	[[Category: Large Structures]]
	[[Category: Goepfert, A]]		[[Category: Goepfert, A]]
	[[Category: Schirmer, T]]		[[Category: Schirmer, T]]

OCA at 07:39, 4 August 2016

2016-08-04T07:39:34Z

←Older revision		Revision as of 07:39, 4 August 2016
Line 1:		Line 1:
		+
	==VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin==		==VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin==
	<StructureSection load='3shg' size='340' side='right' caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3shg' size='340' side='right' caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Barsr Barsr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 ~~Bartonella schoenbuchensis R1~~]), B11C_100027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 ~~Bartonella schoenbuchensis R1~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR]), B11C_100027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 BARSR])</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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [http://www.ebi.ac.uk/pdbsum/3shg 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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [http://pdbe.org/3shg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [http://www.ebi.ac.uk/pdbsum/3shg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3shg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~E6Z0R3_9RHIZ E6Z0R3_9RHIZ~~]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[http://www.uniprot.org/uniprot/~~E6Z0R4_9RHIZ E6Z0R4_9RHIZ~~]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.	+	[[http://www.uniprot.org/uniprot/VBHT_BARSR VBHT_BARSR]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[http://www.uniprot.org/uniprot/VBHA_BARSR VBHA_BARSR]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 19:
	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 3shg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bartonella schoenbuchensis r1~~]]	+	[[Category: Barsr]]
	[[Category: Goepfert, A]]		[[Category: Goepfert, A]]
	[[Category: Schirmer, T]]		[[Category: Schirmer, T]]

OCA at 06:59, 25 December 2014

2014-12-25T06:59:51Z

←Older revision		Revision as of 06:59, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHG FirstGlance]. <br>		<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1]), B11C_100027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1]), B11C_100027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1])</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [http://www.ebi.ac.uk/pdbsum/3shg 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=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [http://www.ebi.ac.uk/pdbsum/3shg PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/E6Z0R3_9RHIZ E6Z0R3_9RHIZ]] Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells. [[http://www.uniprot.org/uniprot/E6Z0R4_9RHIZ E6Z0R4_9RHIZ]] Antitoxin component of a toxin-antitoxin (TA) module VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT; competes with ATP-binding and prevents productive ATP-binding to VbhT.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 16:
	Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.,Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942<ref>PMID:22266942</ref>		Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.,Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942<ref>PMID:22266942</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Bartonella schoenbuchensis r1]]		[[Category: Bartonella schoenbuchensis r1]]
-	[[Category: Goepfert, A.]]	+	[[Category: Goepfert, A]]
-	[[Category: Schirmer, T.]]	+	[[Category: Schirmer, T]]
	[[Category: Adenylylation]]		[[Category: Adenylylation]]
	[[Category: Amp transfer]]		[[Category: Amp transfer]]

OCA at 05:26, 5 June 2014

2014-06-05T05:26:42Z

←Older revision		Revision as of 05:26, 5 June 2014
Line 1:		Line 1:
-	[[~~Image:~~3shg.~~png~~\|~~left~~\|~~200px~~]]	+	==VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin==
		+	<StructureSection load='3shg' size='340' side='right' caption='[[3shg]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2jk8\|2jk8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">B11C_100026 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1]), B11C_100027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=687861 Bartonella schoenbuchensis R1])</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3shg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shg RCSB], [http://www.ebi.ac.uk/pdbsum/3shg PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Fic proteins that are defined by the ubiquitous FIC (filamentation induced by cyclic AMP) domain are known to catalyse adenylylation (also called AMPylation); that is, the transfer of AMP onto a target protein. In mammalian cells, adenylylation of small GTPases through Fic proteins injected by pathogenic bacteria can cause collapse of the actin cytoskeleton and cell death. It is unknown how this potentially deleterious adenylylation activity is regulated in the widespread Fic proteins that are found in all domains of life and that are thought to have critical roles in intrinsic signalling processes. Here we show that FIC-domain-mediated adenylylation is controlled by a conserved mechanism of ATP-binding-site obstruction that involves an inhibitory alpha-helix (alpha(inh)) with a conserved (S/T)XXXE(G/N) motif, and that in this mechanism the invariable glutamate competes with ATP gamma-phosphate binding. Consistent with this, FIC-domain-mediated growth arrest of bacteria by the VbhT toxin of Bartonella schoenbuchensis is intermolecularly repressed by the VbhA antitoxin through tight binding of its alpha(inh) to the FIC domain of VbhT, as shown by structure and function analysis. Furthermore, structural comparisons with other bacterial Fic proteins, such as Fic of Neisseria meningitidis and of Shewanella oneidensis, show that alpha(inh) frequently constitutes an amino-terminal or carboxy-terminal extension to the FIC domain, respectively, partially obstructing the ATP binding site in an intramolecular manner. After mutation of the inhibitory motif in various Fic proteins, including the human homologue FICD (also known as HYPE), adenylylation activity is considerably boosted, consistent with the anticipated relief of inhibition. Structural homology modelling of all annotated Fic proteins indicates that inhibition by alpha(inh) is universal and conserved through evolution, as the inhibitory motif is present in approximately 90% of all putatively adenylylation-active FIC domains, including examples from all domains of life and from viruses. Future studies should reveal how intrinsic or extrinsic factors modulate adenylylation activity by weakening the interaction of alpha(inh) with the FIC active site.

-	<!--	+	Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins.,Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C Nature. 2012 Jan 22;482(7383):107-10. doi: 10.1038/nature10729. PMID:22266942<ref>PMID:22266942</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_3shg"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	-->	+
-	~~{{STRUCTURE_3shg\| PDB=3shg \| SCENE= }}~~	+

-	~~===VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph~~, ~~{{ABSTRACT_PUBMED_22266942}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22266942 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22266942}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3shg]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022266942<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Bartonella schoenbuchensis r1]]		[[Category: Bartonella schoenbuchensis r1]]
	[[Category: Goepfert, A.]]		[[Category: Goepfert, A.]]

OCA at 05:48, 8 February 2012

2012-02-08T05:48:08Z

←Older revision		Revision as of 05:48, 8 February 2012
Line 11:		Line 11:
	===VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin===		===VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22266942}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22266942 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22266942}}

	==About this Structure==		==About this Structure==
	[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA].		[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022266942</ref><references group="xtra"/>
	[[Category: Bartonella schoenbuchensis r1]]		[[Category: Bartonella schoenbuchensis r1]]
	[[Category: Goepfert, A.]]		[[Category: Goepfert, A.]]

OCA at 07:28, 1 February 2012

2012-02-01T07:28:11Z

←Older revision		Revision as of 07:28, 1 February 2012
Line 1:		Line 1:
-	[[Image:3shg.~~jpg~~\|left\|200px]]	+	[[Image:3shg.png\|left\|200px]]

	<!--		<!--

OCA at 06:43, 25 January 2012

2012-01-25T06:43:28Z

←Older revision		Revision as of 06:43, 25 January 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3shg.jpg\|left\|200px]]

-	The ~~entry 3shg~~ is ~~ON HOLD~~ ~~until Jan 24 2013~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3shg", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3shg\| PDB=3shg \| SCENE= }}

-	~~Authors: Goepfert, A., Schirmer, T.~~	+	===VBHT Fic protein from BARTONELLA SCHOENBUCHENSIS in complex with VBHA antitoxin===

-	~~Description~~:	+
		+	==About this Structure==
		+	[[3shg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_schoenbuchensis_r1 Bartonella schoenbuchensis r1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHG OCA].
		+	[[Category: Bartonella schoenbuchensis r1]]
		+	[[Category: Goepfert, A.]]
		+	[[Category: Schirmer, T.]]
		+	[[Category: Adenylylation]]
		+	[[Category: Amp transfer]]
		+	[[Category: Ampylation]]
		+	[[Category: Fic fold]]
		+	[[Category: Toxin-antitoxin complex]]
		+	[[Category: Transferase-protein binding complex]]

OCA at 10:09, 18 January 2012

2012-01-18T10:09:40Z

←Older revision		Revision as of 10:09, 18 January 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3shg is ON HOLD until ~~Paper Publication~~	+	The entry 3shg is ON HOLD until Jan 24 2013

	Authors: Goepfert, A., Schirmer, T.		Authors: Goepfert, A., Schirmer, T.

	Description:		Description:

OCA at 06:11, 20 July 2011

2011-07-20T06:11:40Z

←Older revision		Revision as of 06:11, 20 July 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3shg is ON HOLD	+	The entry 3shg is ON HOLD until Paper Publication

	Authors: Goepfert, A., Schirmer, T.		Authors: Goepfert, A., Schirmer, T.

	Description:		Description: