2vfo - Revision history

OCA at 15:18, 13 December 2023

2023-12-13T15:18:44Z

←Older revision		Revision as of 15:18, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2vfo' size='340' side='right'caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='2vfo' size='340' side='right'caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Bpp22 Bpp22~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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;'>[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [https://pdbe.org/2vfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [https://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo 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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [https://pdbe.org/2vfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [https://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo ProSAT]</span></td></tr>
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[https://www.uniprot.org/uniprot/FIBER_BPP22 FIBER_BPP22] Structural component of the short non-contractile tail. The tail comprises six fibers that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.<ref>PMID:12837775</ref> <ref>PMID:20817910</ref>
-	~~By means of genetic screens, a great number of mutations that affect the folding and stability of the tailspike protein from Salmonella phage P22 have been identified~~. ~~Temperature-sensitive folding (tsf) mutations decrease folding yields at high temperature, but hardly affect thermal stability of the native trimeric structure when assembled at low temperature~~. ~~Global suppressor (su) mutations mitigate this phenotype. Virtually all~~ of ~~these mutations are located in~~ the ~~central domain of tailspike, a large parallel beta~~-~~helix~~. ~~We modified tailspike by rational single amino acid replacements at three sites in order~~ to ~~investigate~~ the ~~influence of mutations of two types:~~ (1) ~~mutations expected to cause a tsf phenotype by increasing the side-chain volume of a core residue,~~ and ~~(2) mutations in a similar structural context as two of the four known su mutations~~, ~~which have been suggested to stabilize folding intermediates and~~ the ~~native structure by the release of backbone strain~~, an effect well known for residues that are primarily evolved for function and not for stability or folding of the protein. Analysis of folding yields, refolding kinetics and thermal denaturation kinetics in vitro show that the tsf phenotype can indeed be produced rationally by increasing the volume of side chains in the beta-~~helix core. The high~~-resolution crystal structure of mutant T326F proves that structural rearrangements only take place in the remarkably plastic lumen of the beta-helix, leaving the arrangement of the hydrogen-bonded backbone and ~~thus the surface~~ of the ~~protein unaffected. This supports the notion that changes in the stability of an intermediate, in which the beta~~-~~helix domain is largely formed, are the essential mechanism by which tsf mutations affect tailspike folding~~. ~~A rational design~~ of ~~su mutants, on~~ the ~~other hand, appears to be more difficult. The exchange of two residues in~~ the ~~active site expected to lead to a drastic release of steric strain neither enhanced~~ the ~~folding properties nor the stability of tailspike~~. Apparently, side-chain interactions in these cases overcompensate for backbone strain, illustrating the extreme optimization of the tailspike protein for conformational stability. The result exemplifies the view arising from the statistical analysis of the distribution of backbone dihedral angles in known three-dimensional protein structures that the adoption of straight phi/psi angles other than the most favorable ones is often caused by side-chain interactions. Proteins 2000;39:89-101.	+
-		+
-	Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.,Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R Proteins. 2000 Apr 1;39(1):89-101. PMID:10737931<ref>PMID:~~10737931~~</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.~~<br>	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 2vfo" style="background-color~~:~~#fffaf0;">~~</~~div~~>	+

	==See Also==		==See Also==
-	*[[Tailspike protein\|Tailspike protein]]	+	*[[Tailspike protein 3D structures\|Tailspike protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Bpp22]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Becker, M]]~~	+	[[Category: Salmonella virus P22]]
-	~~[[Category: Heinemann, U]]~~	+	[[Category: Becker M]]
-	~~[[Category: Mueller, J J]]~~	+	[[Category: Heinemann U]]
-	~~[[Category: Seckler, R]]~~	+	[[Category: Mueller JJ]]
-	~~[[Category: Endoglycosidase]]~~	+	[[Category: Seckler R]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Late protein]]~~	+
-	~~[[Category:~~ P22 ~~tailspike protein~~]]	+
-	[[Category: ~~Protein folding~~]]	+
-	[[Category: ~~Protein stability~~]]	+
-	[[Category: ~~Right-handed parallel beta-helix~~]]	+
-	[[Category: ~~Salmonella bacteriophage p22~~]]	+

OCA at 11:36, 30 March 2022

2022-03-30T11:36:16Z

←Older revision		Revision as of 11:36, 30 March 2022
Line 3:		Line 3:
	<StructureSection load='2vfo' size='340' side='right'caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='2vfo' size='340' side='right'caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2VFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</div></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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [~~http~~://pdbe.org/2vfo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo 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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [https://pdbe.org/2vfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [https://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:51, 25 June 2020

2020-06-25T07:51:52Z

←Older revision		Revision as of 07:51, 25 June 2020
Line 1:		Line 1:

	==Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L==		==Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L==
-	<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='2vfo' size='340' side='right'caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VFO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [http://pdbe.org/2vfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [http://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo 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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [http://pdbe.org/2vfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [http://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 2vfo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2vfo" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tailspike protein\|Tailspike protein]]
	== References ==		== References ==
	<references/>		<references/>
Line 22:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bpp22]]		[[Category: Bpp22]]
		+	[[Category: Large Structures]]
	[[Category: Becker, M]]		[[Category: Becker, M]]
	[[Category: Heinemann, U]]		[[Category: Heinemann, U]]

OCA at 21:13, 19 September 2018

2018-09-19T21:13:03Z

←Older revision		Revision as of 21:13, 19 September 2018
Line 1:		Line 1:

-	==~~LOW TEMPERATURE STRUCTURE OF~~ P22 ~~TAILSPIKE PROTEIN FRAGMENT~~ (109-666), ~~MUTANT~~ V125L==	+	==Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125L==
	<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==

OCA at 09:36, 11 August 2016

2016-08-11T09:36:00Z

←Older revision		Revision as of 09:36, 11 August 2016
Line 1:		Line 1:
		+
	==LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L==		==LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L==
	<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Enterobacteria_phage_p22 Enterobacteria phage p22~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VFO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VFO FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [http://www.ebi.ac.uk/pdbsum/2vfo 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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [http://pdbe.org/2vfo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [http://www.ebi.ac.uk/pdbsum/2vfo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfo ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 15:		Line 16:
	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 2vfo" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Enterobacteria phage p22~~]]	+	[[Category: Bpp22]]
	[[Category: Becker, M]]		[[Category: Becker, M]]
	[[Category: Heinemann, U]]		[[Category: Heinemann, U]]

OCA at 06:36, 22 January 2015

2015-01-22T06:36:31Z

←Older revision		Revision as of 06:36, 22 January 2015
Line 20:		Line 20:
	</StructureSection>		</StructureSection>
	[[Category: Enterobacteria phage p22]]		[[Category: Enterobacteria phage p22]]
-	[[Category: Becker, M.]]	+	[[Category: Becker, M]]
-	[[Category: Heinemann, U.]]	+	[[Category: Heinemann, U]]
-	[[Category: Mueller, J J.]]	+	[[Category: Mueller, J J]]
-	[[Category: Seckler, R.]]	+	[[Category: Seckler, R]]
	[[Category: Endoglycosidase]]		[[Category: Endoglycosidase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 11:25, 20 October 2014

2014-10-20T11:25:15Z

←Older revision		Revision as of 11:25, 20 October 2014
Line 1:		Line 1:
-	[[~~Image:~~2vfo.~~png~~\|~~left~~\|~~200px~~]]	+	==LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L==
		+	<StructureSection load='2vfo' size='340' side='right' caption='[[2vfo]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VFO FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1lkt\|1lkt]], [[1qa1\|1qa1]], [[1qa2\|1qa2]], [[1qa3\|1qa3]], [[1qrb\|1qrb]], [[1tyv\|1tyv]], [[2vfm\|2vfm]], [[1clw\|1clw]], [[1qq1\|1qq1]], [[1qrc\|1qrc]], [[1tsp\|1tsp]], [[2vfn\|2vfn]], [[2vfp\|2vfp]], [[2vfq\|2vfq]]</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=2vfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vfo RCSB], [http://www.ebi.ac.uk/pdbsum/2vfo PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	By means of genetic screens, a great number of mutations that affect the folding and stability of the tailspike protein from Salmonella phage P22 have been identified. Temperature-sensitive folding (tsf) mutations decrease folding yields at high temperature, but hardly affect thermal stability of the native trimeric structure when assembled at low temperature. Global suppressor (su) mutations mitigate this phenotype. Virtually all of these mutations are located in the central domain of tailspike, a large parallel beta-helix. We modified tailspike by rational single amino acid replacements at three sites in order to investigate the influence of mutations of two types: (1) mutations expected to cause a tsf phenotype by increasing the side-chain volume of a core residue, and (2) mutations in a similar structural context as two of the four known su mutations, which have been suggested to stabilize folding intermediates and the native structure by the release of backbone strain, an effect well known for residues that are primarily evolved for function and not for stability or folding of the protein. Analysis of folding yields, refolding kinetics and thermal denaturation kinetics in vitro show that the tsf phenotype can indeed be produced rationally by increasing the volume of side chains in the beta-helix core. The high-resolution crystal structure of mutant T326F proves that structural rearrangements only take place in the remarkably plastic lumen of the beta-helix, leaving the arrangement of the hydrogen-bonded backbone and thus the surface of the protein unaffected. This supports the notion that changes in the stability of an intermediate, in which the beta-helix domain is largely formed, are the essential mechanism by which tsf mutations affect tailspike folding. A rational design of su mutants, on the other hand, appears to be more difficult. The exchange of two residues in the active site expected to lead to a drastic release of steric strain neither enhanced the folding properties nor the stability of tailspike. Apparently, side-chain interactions in these cases overcompensate for backbone strain, illustrating the extreme optimization of the tailspike protein for conformational stability. The result exemplifies the view arising from the statistical analysis of the distribution of backbone dihedral angles in known three-dimensional protein structures that the adoption of straight phi/psi angles other than the most favorable ones is often caused by side-chain interactions. Proteins 2000;39:89-101.

-	~~{{STRUCTURE_2vfo\| PDB=2vfo \| SCENE= }}~~	+	Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein.,Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R Proteins. 2000 Apr 1;39(1):89-101. PMID:10737931<ref>PMID:10737931</ref>

-	~~===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666)~~, ~~MUTANT V125L===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_10737931}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2vfo]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:010737931<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Enterobacteria phage p22]]		[[Category: Enterobacteria phage p22]]
	[[Category: Becker, M.]]		[[Category: Becker, M.]]

OCA: Protected "2vfo" [edit=sysop:move=sysop]

2013-01-07T19:40:35Z

Protected "2vfo" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:40, 7 January 2013

OCA at 19:40, 7 January 2013

2013-01-07T19:40:34Z

←Older revision		Revision as of 19:40, 7 January 2013
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-	{{Seed}}
	[[Image:2vfo.png\|left\|200px]]		[[Image:2vfo.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2vfo\| PDB=2vfo \| SCENE= }}		{{STRUCTURE_2vfo\| PDB=2vfo \| SCENE= }}

	===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L===		===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L===

		+	{{ABSTRACT_PUBMED_10737931}}

	==About this Structure==		==About this Structure==
-	~~2VFO~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA].	+	[[2vfo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VFO OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~10737931~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010737931</ref><references group="xtra"/>
	[[Category: Enterobacteria phage p22]]		[[Category: Enterobacteria phage p22]]
	[[Category: Becker, M.]]		[[Category: Becker, M.]]
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	[[Category: Right-handed parallel beta-helix]]		[[Category: Right-handed parallel beta-helix]]
	[[Category: Salmonella bacteriophage p22]]		[[Category: Salmonella bacteriophage p22]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jan 25 07:34:57 2009''

OCA at 05:34, 25 January 2009

2009-01-25T05:34:58Z

←Older revision		Revision as of 05:34, 25 January 2009
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	{{Seed}}		{{Seed}}
-	[[Image:2vfo.~~jpg~~\|left\|200px]]	+	[[Image:2vfo.png\|left\|200px]]

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	===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L===		===LOW TEMPERATURE STRUCTURE OF P22 TAILSPIKE PROTEIN FRAGMENT (109-666), MUTANT V125L===

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-	<!--
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-	(as it appears on PubMed at http://www.pubmed.gov), where 10737931 is the PubMed ID number.
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-	{{ABSTRACT_PUBMED_10737931}}

	==About this Structure==		==About this Structure==
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	==Reference==		==Reference==
-	Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein., Schuler B, Furst F, Osterroth F, Steinbacher S, Huber R, Seckler R, Proteins. 2000 Apr 1;39(1):89-101. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/10737931 10737931]~~	+	<ref group="xtra">PMID:10737931</ref><references group="xtra"/>
	[[Category: Enterobacteria phage p22]]		[[Category: Enterobacteria phage p22]]
	[[Category: Becker, M.]]		[[Category: Becker, M.]]
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	[[Category: Salmonella bacteriophage p22]]		[[Category: Salmonella bacteriophage p22]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Dec 17 13~~:14:~~30 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jan 25 07:34:57 2009''