1s5g
From Proteopedia
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| - | [[Image:1s5g.gif|left|200px]] | + | [[Image:1s5g.gif|left|200px]] |
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| - | '''Structure of Scallop myosin S1 reveals a novel nucleotide conformation''' | + | {{Structure |
| + | |PDB= 1s5g |SIZE=350|CAPTION= <scene name='initialview01'>1s5g</scene>, resolution 3.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of Scallop myosin S1 reveals a novel nucleotide conformation''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S5G is a [ | + | 1S5G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S5G OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15184651 15184651] |
[[Category: Argopecten irradians]] | [[Category: Argopecten irradians]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: scallop myosin s1]] | [[Category: scallop myosin s1]] | ||
| - | ''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 14:00:41 2008'' |
Revision as of 12:00, 20 March 2008
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| , resolution 3.1Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Scallop myosin S1 reveals a novel nucleotide conformation
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
1S5G 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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