3bas
From Proteopedia
(New page: 200px<br /><applet load="3bas" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bas, resolution 2.300Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the | + | The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the two heads of this dimeric molecule and is key to its function. Previously, a crystal structure of this predominantly coiled-coil region was determined for a short fragment (51 residues plus a leucine zipper) of the scallop striated muscle myosin isoform. In that study, the N-terminal 10-14 residues were found to be disordered. We have now determined the structure of the same scallop peptide in three additional crystal environments. In each of two of these structures, improved order has allowed visualization of the entire N-terminus in one chain of the dimeric peptide. We have also compared the melting temperatures of this scallop S2 peptide with those of analogous peptides from three other isoforms. Taken together, these experiments, along with examination of sequences, point to a diminished stability of the N-terminal region of S2 in regulated myosins, compared with those myosins whose regulation is thin filament linked. It seems plain that this isoform-specific instability promotes the off-state conformation of the heads in regulated myosins. We also discuss how myosin isoforms with varied thermal stabilities share the basic capacity to transmit force efficiently in order to produce contraction in their on states. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Argopecten irradians, saccharomyces cerevisiae]] | [[Category: Argopecten irradians, saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brown, J | + | [[Category: Brown, J H.]] |
[[Category: Cohen, C.]] | [[Category: Cohen, C.]] | ||
[[Category: IOD]] | [[Category: IOD]] | ||
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[[Category: thick filament]] | [[Category: thick filament]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:31 2008'' |
Revision as of 17:04, 21 February 2008
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Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form
Overview
The N-terminal region of myosin's rod-like subfragment 2 (S2) joins the two heads of this dimeric molecule and is key to its function. Previously, a crystal structure of this predominantly coiled-coil region was determined for a short fragment (51 residues plus a leucine zipper) of the scallop striated muscle myosin isoform. In that study, the N-terminal 10-14 residues were found to be disordered. We have now determined the structure of the same scallop peptide in three additional crystal environments. In each of two of these structures, improved order has allowed visualization of the entire N-terminus in one chain of the dimeric peptide. We have also compared the melting temperatures of this scallop S2 peptide with those of analogous peptides from three other isoforms. Taken together, these experiments, along with examination of sequences, point to a diminished stability of the N-terminal region of S2 in regulated myosins, compared with those myosins whose regulation is thin filament linked. It seems plain that this isoform-specific instability promotes the off-state conformation of the heads in regulated myosins. We also discuss how myosin isoforms with varied thermal stabilities share the basic capacity to transmit force efficiently in order to produce contraction in their on states.
About this Structure
3BAS is a Single protein structure of sequence from Argopecten irradians, saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.
Reference
An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins., Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C, J Mol Biol. 2008 Feb 1;375(5):1434-43. Epub 2007 Nov 28. PMID:18155233
Page seeded by OCA on Thu Feb 21 19:04:31 2008
Categories: Argopecten irradians, saccharomyces cerevisiae | Single protein | Brown, J H. | Cohen, C. | IOD | Actin-binding | Alpha-helical coiled coil | Atp-binding | Calmodulin-binding | Contractile protein | Cytoplasm | Disorder | Motor protein | Muscle protein | Myosin | Nucleotide-binding | Salt links | Thick filament
