1tmz
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmz OCA], [http://www.ebi.ac.uk/pdbsum/1tmz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tmz RCSB]</span> | ||
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[[Category: tropomyosin]] | [[Category: tropomyosin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:25 2008'' |
Revision as of 20:58, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TMZIP: A CHIMERIC PEPTIDE MODEL OF THE N-TERMINUS OF ALPHA TROPOMYOSIN, NMR, 15 STRUCTURES
Overview
Tropomyosins (TMs) are highly conserved, coiled-coil, actin binding regulatory proteins found in most eukaryotic cells. The amino-terminal domain of 284-residue TMs is among the most conserved and functionally important regions. The first nine residues are proposed to bind to the carboxyl-terminal nine residues to form the "overlap" region between successive TMs, which bind along the actin filament. Here, the structure of the N-terminus of muscle alpha-TM, in a chimeric peptide, TMZip, has been solved using circular dichroism (CD) and two-dimensional proton nuclear magnetic resonance (2D 1H NMR) spectroscopy. Residues 1-14 of TMZip are the first 14 N-terminal residues of rabbit striated alpha-TM, and residues 15-32 of TMZip are the last 18 C-terminal residues of the yeast GCN4 transcription factor. CD measurements show that TMZip forms a two-stranded coiled-coil alpha-helix with an enthalpy of folding of -34 +/- 2 kcal/mol. In 2D1H NMR studies at 15 degrees C, pH 6.4, the peptide exhibits 123 sequential and medium range intrachain NOE cross peaks per chain, characteristic of alpha-helices extending from residue 1 to residue 29, together with 85 long-range NOE cross peaks arising from interchain interactions. The three-dimensional structure of TMZip has been determined using these data plus an additional 509 intrachain constraints per chain. The coiled-coil domain extends to the N-terminus. Amide hydrogen exchange studies, however, suggest that the TM region is less stable than the GCN4 region. The work reported here is the first atomic-resolution structure of any region of TM and it allows insight into the mechanism of the function of the highly conserved N-terminal domain.
About this Structure
1TMZ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The structure of the N-terminus of striated muscle alpha-tropomyosin in a chimeric peptide: nuclear magnetic resonance structure and circular dichroism studies., Greenfield NJ, Montelione GT, Farid RS, Hitchcock-DeGregori SE, Biochemistry. 1998 May 26;37(21):7834-43. PMID:9601044
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