1kql
From Proteopedia
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| - | [[Image:1kql.gif|left|200px]] | + | [[Image:1kql.gif|left|200px]] |
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| - | '''Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution''' | + | {{Structure |
| + | |PDB= 1kql |SIZE=350|CAPTION= <scene name='initialview01'>1kql</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1KQL is a [ | + | 1KQL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_and_rattus_norvegicus Saccharomyces cerevisiae and rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQL OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site., Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:[http:// | + | The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site., Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12032291 12032291] |
[[Category: Saccharomyces cerevisiae and rattus norvegicus]] | [[Category: Saccharomyces cerevisiae and rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tropomyosin]] | [[Category: tropomyosin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:20:54 2008'' |
Revision as of 10:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution
Overview
Contraction in striated and cardiac muscles is regulated by the motions of a Ca(2+)-sensitive tropomyosin/troponin switch. In contrast, troponin is absent in other muscle types and in nonmuscle cells, and actomyosin regulation is myosin-linked. Here we report an unusual crystal structure at 2.7 A of the C-terminal 31 residues of rat striated-muscle alpha-tropomyosin (preceded by a fragment of the GCN4 leucine zipper). The C-terminal 22 residues (263-284) of the structure do not form a two-stranded alpha-helical coiled coil as does the rest of the molecule, but here the alpha-helices splay apart and are stabilized by the formation of a tail-to-tail dimer with a symmetry-related molecule. The site of splaying involves a small group of destabilizing core residues that is present only in striated muscle tropomyosin isoforms. These results reveal a specific recognition site for troponin T and clarify the physical basis for the unique regulatory mechanism of striated muscles.
About this Structure
1KQL is a Single protein structure of sequence from Saccharomyces cerevisiae and rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site., Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:12032291
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