1qvi
From Proteopedia
(New page: 200px<br /><applet load="1qvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qvi, resolution 2.54Å" /> '''Crystal structure of...) |
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| - | [[Image:1qvi.gif|left|200px]]<br /><applet load="1qvi" size=" | + | [[Image:1qvi.gif|left|200px]]<br /><applet load="1qvi" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qvi, resolution 2.54Å" /> | caption="1qvi, resolution 2.54Å" /> | ||
'''Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head'''<br /> | '''Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have extended the X-ray structure determination of the complete scallop | + | We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 A resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called "pliant region" at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the "internally uncoupled" state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins. |
==About this Structure== | ==About this Structure== | ||
| - | 1QVI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with MG, VO4, CA and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QVI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=VO4:'>VO4</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QVI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Argopecten irradians]] | [[Category: Argopecten irradians]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Brown, J | + | [[Category: Brown, J H.]] |
[[Category: Cohen, C.]] | [[Category: Cohen, C.]] | ||
[[Category: Gourinath, S.]] | [[Category: Gourinath, S.]] | ||
| - | [[Category: Himmel, D | + | [[Category: Himmel, D M.]] |
[[Category: Reshetnikova, L.]] | [[Category: Reshetnikova, L.]] | ||
| - | [[Category: Szent-Gyrgyi, A | + | [[Category: Szent-Gyrgyi, A G.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: sh1 helix]] | [[Category: sh1 helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:08 2008'' |
Revision as of 12:44, 21 February 2008
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Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head
Overview
We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 A resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called "pliant region" at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the "internally uncoupled" state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.
About this Structure
1QVI is a Protein complex structure of sequences from Argopecten irradians with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of scallop Myosin s1 in the pre-power stroke state to 2.6 a resolution: flexibility and function in the head., Gourinath S, Himmel DM, Brown JH, Reshetnikova L, Szent-Gyorgyi AG, Cohen C, Structure. 2003 Dec;11(12):1621-7. PMID:14656445
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