3bas

From Proteopedia

Crystal structure of the N-terminal region of the scallop myosin rod, monoclinic (C2) form

PDB ID 3bas

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Structural highlights

3bas is a 2 chain structure with sequence from Argopecten irradians and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GCN4_YEAST Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.MYS_ARGIR Muscle contraction. Myosin is a protein that binds to F-actin and has ATPase activity that is activated by F-actin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brown JH, Yang Y, Reshetnikova L, Gourinath S, Suveges D, Kardos J, Hobor F, Reutzel R, Nyitray L, Cohen C. An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins. J Mol Biol. 2008 Feb 1;375(5):1434-43. Epub 2007 Nov 28. PMID:18155233 doi:10.1016/j.jmb.2007.11.071