1wdc
From Proteopedia
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| - | [[Image:1wdc.gif|left|200px]] | + | [[Image:1wdc.gif|left|200px]] |
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| - | '''SCALLOP MYOSIN REGULATORY DOMAIN''' | + | {{Structure |
| + | |PDB= 1wdc |SIZE=350|CAPTION= <scene name='initialview01'>1wdc</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SCALLOP MYOSIN REGULATORY DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WDC is a [ | + | 1WDC 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=1WDC OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation., Houdusse A, Cohen C, Structure. 1996 Jan 15;4(1):21-32. PMID:[http:// | + | Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation., Houdusse A, Cohen C, Structure. 1996 Jan 15;4(1):21-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805510 8805510] |
[[Category: Argopecten irradians]] | [[Category: Argopecten irradians]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: myosin]] | [[Category: myosin]] | ||
| - | ''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 14:55:37 2008'' |
Revision as of 12:55, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SCALLOP MYOSIN REGULATORY DOMAIN
Overview
BACKGROUND: In contrast to the myosins of vertebrate skeletal muscle, molluscan myosins are regulated molecules whose enzymatic activity is switched on by the direct binding of Ca2+. The head portion (S1) of the molecule consists of a motor domain and a regulatory domain (RD) containing a 'regulatory' and an 'essential' light chain (RLC and ELC, respectively). The structures of scallop myosin RD with bound Ca2+, as well as the S1 fragment of chicken skeletal muscle myosin, have been determined previously to 2.8 A resolution. RESULTS: We have determined the structure at 2.0 A resolution of scallop myosin RD with bound Ca2+. The unusual coordination at the specific Ca(2+)-binding site in the ELC has now been clarified, as has the structural basis for Mg2+ binding to the RLC. A comparison of the scallop RD structure with that in the chicken S1 structure shows differences in the bending of the two RDs in two different places. CONCLUSIONS: Based on these structural results, a model for regulation is proposed in which the Ca(2+)-bound RD is a rigid structure, and transient flexibility of the Ca(2+)-free RD allows the myosin heads to make stabilizing intramolecular linkage which shut off the motor.
About this Structure
1WDC is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.
Reference
Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation., Houdusse A, Cohen C, Structure. 1996 Jan 15;4(1):21-32. PMID:8805510
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