1sr6
From Proteopedia
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|PDB= 1sr6 |SIZE=350|CAPTION= <scene name='initialview01'>1sr6</scene>, resolution 2.75Å | |PDB= 1sr6 |SIZE=350|CAPTION= <scene name='initialview01'>1sr6</scene>, resolution 2.75Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1s5g|1S5G]], [[1qvi|1QVI]], [[1kk8|1KK8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sr6 OCA], [http://www.ebi.ac.uk/pdbsum/1sr6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sr6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Risal, D.]] | [[Category: Risal, D.]] | ||
[[Category: Szent-Gyorgyi, A G.]] | [[Category: Szent-Gyorgyi, A G.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
[[Category: complex salt bridge]] | [[Category: complex salt bridge]] | ||
[[Category: near rigor]] | [[Category: near rigor]] | ||
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[[Category: scallop myosin s1]] | [[Category: scallop myosin s1]] | ||
| - | ''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 23:45:54 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1S5G, 1QVI, 1KK8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of nucleotide-free scallop myosin S1
Overview
Structural studies of myosin have indicated some of the conformational changes that occur in this protein during the contractile cycle, and we have now observed a conformational change in a bound nucleotide as well. The 3.1-A x-ray structure of the scallop myosin head domain (subfragment 1) in the ADP-bound near-rigor state (lever arm =45 degrees to the helical actin axis) shows the diphosphate moiety positioned on the surface of the nucleotide-binding pocket, rather than deep within it as had been observed previously. This conformation strongly suggests a specific mode of entry and exit of the nucleotide from the nucleotide-binding pocket through the so-called "front door." In addition, using a variety of scallop structures, including a relatively high-resolution 2.75-A nucleotide-free near-rigor structure, we have identified a conserved complex salt bridge connecting the 50-kDa upper and N-terminal subdomains. This salt bridge is present only in crystal structures of muscle myosin isoforms that exhibit a strong reciprocal relationship (also known as coupling) between actin and nucleotide affinity.
About this Structure
1SR6 is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.
Reference
Myosin subfragment 1 structures reveal a partially bound nucleotide and a complex salt bridge that helps couple nucleotide and actin binding., Risal D, Gourinath S, Himmel DM, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8930-5. Epub 2004 Jun 7. PMID:15184651
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