1tsp
From Proteopedia
(New page: 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=" | + | [[Image:1tsp.jpg|left|200px]]<br /><applet load="1tsp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tsp, resolution 2.0Å" /> | caption="1tsp, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER'''<br /> | '''CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1TSP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: late protein]] | [[Category: late protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:54 2008'' |
Revision as of 13:16, 21 February 2008
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CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER
Overview
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.
About this Structure
1TSP is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
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:8023158
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