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New page: left|200px<br /><applet load="1tsp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tsp, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1tsp.jpg|left|200px]]<br /><applet load="1tsp" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tsp, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER'''<br />


==Overview==
==CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER==
The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part, of the apparatus by which the phage attaches to the bacterial host and, hydrolyzes the O antigen. It has served as a model system for genetic and, biochemical analysis of protein folding. The x-ray structure of a, shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom, resolution. Each subunit of the homotrimer contains a large parallel beta, helix. The interdigitation of the polypeptide chains at the carboxyl, termini is important to protrimer formation in the folding pathway and to, thermostability of the mature protein.
<StructureSection load='1tsp' size='340' side='right'caption='[[1tsp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tsp]] 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=1TSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TSP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=1tsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tsp OCA], [https://pdbe.org/1tsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tsp RCSB], [https://www.ebi.ac.uk/pdbsum/1tsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tsp ProSAT]</span></td></tr>
</table>
== Function ==
[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>


==About this Structure==
==See Also==
1TSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TSP OCA].
*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer., Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P, Science. 1994 Jul 15;265(5170):383-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8023158 8023158]
__TOC__
[[Category: Single protein]]
</StructureSection>
[[Category: Yersinia phage py54]]
[[Category: Large Structures]]
[[Category: Huber, R.]]
[[Category: Salmonella virus P22]]
[[Category: Miller, S.]]
[[Category: Huber R]]
[[Category: Reinemer, P.]]
[[Category: Miller S]]
[[Category: Seckler, R.]]
[[Category: Reinemer P]]
[[Category: Steinbacher, S.]]
[[Category: Seckler R]]
[[Category: Steipe, B.]]
[[Category: Steinbacher S]]
[[Category: late protein]]
[[Category: Steipe B]]
 
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