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2vfn

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Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A

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Retrieved from "http://52.214.119.220/wiki/index.php/2vfn"

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 <StructureSection load='2vfn' size='340' side='right'caption='[[2vfn]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vfn]] 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=2VFN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VFN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vfn]] 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=2VFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VFN 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]] 1.5&#8491;</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]], [[2vfo|2vfo]], [[2vfp|2vfp]], [[2vfq|2vfq]]</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'>[http://proteopedia.org/fgij/fg.htm?mol=2vfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfn OCA], [http://pdbe.org/2vfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vfn RCSB], [http://www.ebi.ac.uk/pdbsum/2vfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfn 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=2vfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfn OCA], [https://pdbe.org/2vfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vfn RCSB], [https://www.ebi.ac.uk/pdbsum/2vfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vfn ProSAT]</span></td></tr>
 </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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2vfn" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Tailspike protein|Tailspike protein]]
+*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bpp22]]
 [[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]]

2vfn

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Low Temperature Structure of P22 Tailspike Protein Fragment (109-666), Mutant V125A

Structural highlights

Function

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References

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