3tmc - Revision history

OCA at 10:10, 1 March 2024

2024-03-01T10:10:10Z

←Older revision		Revision as of 10:10, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3tmc' size='340' side='right'caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='3tmc' size='340' side='right'caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bdeba Bdeba~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_HD100 Bdellovibrio bacteriovorus HD100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMC FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>~~, ~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.55Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]~~</~~div~~><~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<~~tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">Bd1817 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])~~</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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [https://pdbe.org/3tmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [https://www.ebi.ac.uk/pdbsum/3tmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmc 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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [https://pdbe.org/3tmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [https://www.ebi.ac.uk/pdbsum/3tmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmc ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/Q6MM30_BDEBA Q6MM30_BDEBA]
-	Cyclic-di-GMP is a near-ubiquitous bacterial second messenger that is important in localized signal transmission during the control of various processes, including virulence and switching between planktonic and biofilm-based lifestyles. Cyclic-di-GMP is synthesized by GGDEF diguanylate cyclases and hydrolyzed by EAL or HD-GYP phosphodiesterases, with each functional domain often appended to distinct sensory modules. HD-GYP domain proteins have resisted structural analysis, but here we present the first structural representative of this family (1.28 A), obtained using the unusual Bd1817 HD-GYP protein from the predatory bacterium Bdellovibrio bacteriovorus. Bd1817 lacks the active-site tyrosine present in most HD-GYP family members yet remains an excellent model of their features, sharing 48% sequence similarity with the archetype RpfG. The protein structure is highly modular and thus provides a basis for delineating domain boundaries in other stimulus-dependent homologues. Conserved residues in the HD-GYP family cluster around a binuclear metal center, which is observed complexed to a molecule of phosphate, providing information on the mode of hydroxide ion attack on substrate. The fold and active site of the HD-GYP domain are different from those of EAL proteins, and restricted access to the active-site cleft is indicative of a different mode of activity regulation. The region encompassing the GYP motif has a novel conformation and is surface exposed and available for complexation with binding partners, including GGDEF proteins. IMPORTANCE: It is becoming apparent that many bacteria use the signaling molecule cyclic-di-GMP to regulate a variety of processes, most notably, transitions between motility and sessility. Importantly, this regulation is central to several traits implicated in chronic disease (adhesion, biofilm formation, and virulence gene expression). The mechanisms of cyclic-di-GMP synthesis via GGDEF enzymes and hydrolysis via EAL enzymes have been suggested by the analysis of several crystal structures, but no information has been available to date for the unrelated HD-GYP class of hydrolases. Here we present the multidomain structure of an unusual member of the HD-GYP family from the predatory bacterium Bdellovibrio bacteriovorus and detail the features that distinguish it from the wider structural family of general HD fold hydrolases. The structure reveals how a binuclear iron center is formed from several conserved residues and provides a basis for understanding HD-GYP family sequence requirements for c-di-GMP hydrolysis.	+
-		+
-	The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases.,Lovering AL, Capeness MJ, Lambert C, Hobley L, Sockett RE MBio. 2011 Oct 11;2(5). pii: e00163-11. doi: 10.1128/~~mBio.00163-11. Print 2011. PMID:21990613<ref>PMID:21990613<~~/~~ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U~~.S. ~~National Library of Medicine.<br>~~	+
-	</~~div>~~	+
-	~~<div class="pdbe-citations 3tmc" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references~~/>	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bdeba~~]]	+	[[Category: Bdellovibrio bacteriovorus HD100]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lovering~~, A L]]~~	+	[[Category: Lovering AL]]
-	~~[[Category: Hd-gyp]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Phosphodiesterase]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Unknown function~~]]	+

OCA at 17:04, 6 July 2022

2022-07-06T17:04:16Z

←Older revision		Revision as of 17:04, 6 July 2022
Line 1:		Line 1:

	==Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus==		==Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus==
-	<StructureSection load='3tmc' size='340' side='right' caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='3tmc' size='340' side='right'caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TMC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Bd1817 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Bd1817 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [~~http~~://pdbe.org/3tmc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3tmc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmc 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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [https://pdbe.org/3tmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [https://www.ebi.ac.uk/pdbsum/3tmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmc ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Bdeba]]		[[Category: Bdeba]]
		+	[[Category: Large Structures]]
	[[Category: Lovering, A L]]		[[Category: Lovering, A L]]
	[[Category: Hd-gyp]]		[[Category: Hd-gyp]]

OCA at 19:46, 4 August 2016

2016-08-04T19:46:23Z

←Older revision		Revision as of 19:46, 4 August 2016
Line 1:		Line 1:
		+
	==Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus==		==Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus==
	<StructureSection load='3tmc' size='340' side='right' caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='3tmc' size='340' side='right' caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bdellovibrio_bacteriovorus_hd100 Bdellovibrio bacteriovorus hd100~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TMC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bdeba Bdeba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TMC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Bd1817 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 ~~Bdellovibrio bacteriovorus HD100~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Bd1817 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 BDEBA])</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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [http://www.ebi.ac.uk/pdbsum/3tmc 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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [http://pdbe.org/3tmc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [http://www.ebi.ac.uk/pdbsum/3tmc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tmc ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 3tmc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bdellovibrio bacteriovorus hd100~~]]	+	[[Category: Bdeba]]
	[[Category: Lovering, A L]]		[[Category: Lovering, A L]]
	[[Category: Hd-gyp]]		[[Category: Hd-gyp]]

OCA at 07:19, 21 December 2014

2014-12-21T07:19:34Z

←Older revision		Revision as of 07:19, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3tmc\| PDB=3tmc \| SCENE= }}~~	+	==Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus==
-	===Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus===	+	<StructureSection load='3tmc' size='340' side='right' caption='[[3tmc]], [[Resolution\|resolution]] 1.55Å' scene=''>
-	~~{{ABSTRACT_PUBMED_21990613}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3tmc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_hd100 Bdellovibrio bacteriovorus hd100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TMC FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3tm8\|3tm8]], [[3tmb\|3tmb]], [[3tmd\|3tmd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Bd1817 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264462 Bdellovibrio bacteriovorus HD100])</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=3tmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tmc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tmc RCSB], [http://www.ebi.ac.uk/pdbsum/3tmc PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cyclic-di-GMP is a near-ubiquitous bacterial second messenger that is important in localized signal transmission during the control of various processes, including virulence and switching between planktonic and biofilm-based lifestyles. Cyclic-di-GMP is synthesized by GGDEF diguanylate cyclases and hydrolyzed by EAL or HD-GYP phosphodiesterases, with each functional domain often appended to distinct sensory modules. HD-GYP domain proteins have resisted structural analysis, but here we present the first structural representative of this family (1.28 A), obtained using the unusual Bd1817 HD-GYP protein from the predatory bacterium Bdellovibrio bacteriovorus. Bd1817 lacks the active-site tyrosine present in most HD-GYP family members yet remains an excellent model of their features, sharing 48% sequence similarity with the archetype RpfG. The protein structure is highly modular and thus provides a basis for delineating domain boundaries in other stimulus-dependent homologues. Conserved residues in the HD-GYP family cluster around a binuclear metal center, which is observed complexed to a molecule of phosphate, providing information on the mode of hydroxide ion attack on substrate. The fold and active site of the HD-GYP domain are different from those of EAL proteins, and restricted access to the active-site cleft is indicative of a different mode of activity regulation. The region encompassing the GYP motif has a novel conformation and is surface exposed and available for complexation with binding partners, including GGDEF proteins. IMPORTANCE: It is becoming apparent that many bacteria use the signaling molecule cyclic-di-GMP to regulate a variety of processes, most notably, transitions between motility and sessility. Importantly, this regulation is central to several traits implicated in chronic disease (adhesion, biofilm formation, and virulence gene expression). The mechanisms of cyclic-di-GMP synthesis via GGDEF enzymes and hydrolysis via EAL enzymes have been suggested by the analysis of several crystal structures, but no information has been available to date for the unrelated HD-GYP class of hydrolases. Here we present the multidomain structure of an unusual member of the HD-GYP family from the predatory bacterium Bdellovibrio bacteriovorus and detail the features that distinguish it from the wider structural family of general HD fold hydrolases. The structure reveals how a binuclear iron center is formed from several conserved residues and provides a basis for understanding HD-GYP family sequence requirements for c-di-GMP hydrolysis.

-	~~==About this Structure==~~	+	The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases.,Lovering AL, Capeness MJ, Lambert C, Hobley L, Sockett RE MBio. 2011 Oct 11;2(5). pii: e00163-11. doi: 10.1128/mBio.00163-11. Print 2011. PMID:21990613<ref>PMID:21990613</ref>
-	~~[[3tmc]] is a 2 chain~~ structure ~~with sequence~~ from ~~[http://en~~.~~wikipedia~~.~~org/wiki/Bdellovibrio_bacteriovorus_hd100 Bdellovibrio bacteriovorus hd100]~~. ~~Full crystallographic information is available from [http~~:~~//oca~~.~~weizmann.ac~~.il/~~oca~~-~~bin/ocashort?id=3TMC OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:021990613</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bdellovibrio bacteriovorus hd100]]		[[Category: Bdellovibrio bacteriovorus hd100]]
-	[[Category: Lovering, A L.]]	+	[[Category: Lovering, A L]]
	[[Category: Hd-gyp]]		[[Category: Hd-gyp]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 08:56, 19 June 2013

2013-06-19T08:56:31Z

←Older revision		Revision as of 08:56, 19 June 2013
Line 1:		Line 1:
-	[[Image:3tmc.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3tmc", 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.
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	{{STRUCTURE_3tmc\| PDB=3tmc \| SCENE= }}		{{STRUCTURE_3tmc\| PDB=3tmc \| SCENE= }}
-
	===Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus===		===Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus===
		+	{{ABSTRACT_PUBMED_21990613}}

		+	==About this Structure==
		+	[[3tmc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus_hd100 Bdellovibrio bacteriovorus hd100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA].

-	==~~About this Structure~~==	+	==Reference==
-	~~[[3tmc]] is a 2 chain structure with sequence from [http~~://~~en.wikipedia.org~~/~~wiki/Bdellovibrio_bacteriovorus Bdellovibrio bacteriovorus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA].~~	+	<ref group="xtra">PMID:021990613</ref><references group="xtra"/><references/>
-	[[Category: Bdellovibrio bacteriovorus]]	+	[[Category: Bdellovibrio bacteriovorus hd100]]
	[[Category: Lovering, A L.]]		[[Category: Lovering, A L.]]
	[[Category: Hd-gyp]]		[[Category: Hd-gyp]]

OCA at 10:23, 30 October 2011

2011-10-30T10:23:49Z

←Older revision		Revision as of 10:23, 30 October 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3tmc.png\|left\|200px]]

-	The ~~entry 3tmc~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3tmc", 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_3tmc\| PDB=3tmc \| SCENE= }}

-	~~Authors: Lovering~~, ~~A.L.~~	+	===Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus===

-	~~Description: Bd1817,~~ a ~~HDG"Y"P protein~~ from Bdellovibrio bacteriovorus	+
		+	==About this Structure==
		+	[[3tmc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bdellovibrio_bacteriovorus Bdellovibrio bacteriovorus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TMC OCA].
		+	[[Category: Bdellovibrio bacteriovorus]]
		+	[[Category: Lovering, A L.]]
		+	[[Category: Hd-gyp]]
		+	[[Category: Hydrolase]]
		+	[[Category: Phosphodiesterase]]
		+	[[Category: Signaling protein]]
		+	[[Category: Unknown function]]

OCA at 05:31, 21 September 2011

2011-09-21T05:31:18Z

←Older revision		Revision as of 05:31, 21 September 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Lovering, A.L.		Authors: Lovering, A.L.

	Description: Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus		Description: Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus

OCA: Protected "3tmc" [edit=sysop:move=sysop]

2011-09-07T05:50:48Z

Protected "3tmc" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:50, 7 September 2011

OCA: New page: '''Unreleased structure''' The entry 3tmc is ON HOLD Authors: Lovering, A.L. Description: Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus

2011-09-07T05:50:47Z

New page: '''Unreleased structure''' The entry 3tmc is ON HOLD Authors: Lovering, A.L. Description: Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus

New page

'''Unreleased structure'''

The entry 3tmc is ON HOLD

Authors: Lovering, A.L.

Description: Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus