1kqm
From Proteopedia
(New page: 200px<br /><applet load="1kqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kqm, resolution 3.00Å" /> '''SCALLOP MYOSIN S1-AM...) |
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| - | [[Image:1kqm.gif|left|200px]]<br /><applet load="1kqm" size=" | + | [[Image:1kqm.gif|left|200px]]<br /><applet load="1kqm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kqm, resolution 3.00Å" /> | caption="1kqm, resolution 3.00Å" /> | ||
'''SCALLOP MYOSIN S1-AMPPNP IN THE ACTIN-DETACHED CONFORMATION'''<br /> | '''SCALLOP MYOSIN S1-AMPPNP IN THE ACTIN-DETACHED CONFORMATION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we report a 2.3-A crystal structure of scallop myosin S1 complexed | + | Here we report a 2.3-A crystal structure of scallop myosin S1 complexed with ADP.BeF(x), as well as three additional structures (at 2.8-3.8 A resolution) for this S1 complexed with ATP analogs, some of which are cross-linked by para-phenyl dimaleimide, a short intramolecular cross-linker. In all cases, the complexes are characterized by an unwound SH1 helix first seen in an unusual 2.5-A scallop myosin-MgADP structure and described as corresponding to a previously unrecognized actin-detached internally uncoupled state. The unwinding of the SH1 helix effectively uncouples the converter/lever arm module from the motor and allows cross-linking by para-phenyl dimaleimide, which has been shown to occur only in weak actin-binding states of the molecule. Mutations near the metastable SH1 helix that disable the motor can be accounted for by viewing this structural element as a clutch controlling the transmission of torque to the lever arm. We have also determined a 3.2-A nucleotide-free structure of scallop myosin S1, which suggests that in the near-rigor state there are two conformations in the switch I loop, depending on whether nucleotide is present. Analysis of the subdomain motions in the weak actin-binding states revealed by x-ray crystallography, together with recent electron microscopic results, clarify the mechanical roles of the parts of the motor in the course of the contractile cycle and suggest how strong binding to actin triggers both the power stroke and product release. |
==About this Structure== | ==About this Structure== | ||
| - | 1KQM 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 CA, MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1KQM 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=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQM OCA]. |
==Reference== | ==Reference== | ||
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[[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: Shen, Y.]] | [[Category: Shen, Y.]] | ||
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[[Category: myosin]] | [[Category: myosin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:00 2008'' |
Revision as of 11:37, 21 February 2008
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SCALLOP MYOSIN S1-AMPPNP IN THE ACTIN-DETACHED CONFORMATION
Overview
Here we report a 2.3-A crystal structure of scallop myosin S1 complexed with ADP.BeF(x), as well as three additional structures (at 2.8-3.8 A resolution) for this S1 complexed with ATP analogs, some of which are cross-linked by para-phenyl dimaleimide, a short intramolecular cross-linker. In all cases, the complexes are characterized by an unwound SH1 helix first seen in an unusual 2.5-A scallop myosin-MgADP structure and described as corresponding to a previously unrecognized actin-detached internally uncoupled state. The unwinding of the SH1 helix effectively uncouples the converter/lever arm module from the motor and allows cross-linking by para-phenyl dimaleimide, which has been shown to occur only in weak actin-binding states of the molecule. Mutations near the metastable SH1 helix that disable the motor can be accounted for by viewing this structural element as a clutch controlling the transmission of torque to the lever arm. We have also determined a 3.2-A nucleotide-free structure of scallop myosin S1, which suggests that in the near-rigor state there are two conformations in the switch I loop, depending on whether nucleotide is present. Analysis of the subdomain motions in the weak actin-binding states revealed by x-ray crystallography, together with recent electron microscopic results, clarify the mechanical roles of the parts of the motor in the course of the contractile cycle and suggest how strong binding to actin triggers both the power stroke and product release.
About this Structure
1KQM is a Protein complex structure of sequences from Argopecten irradians with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor., Himmel DM, Gourinath S, Reshetnikova L, Shen Y, Szent-Gyorgyi AG, Cohen C, Proc Natl Acad Sci U S A. 2002 Oct 1;99(20):12645-50. Epub 2002 Sep 24. PMID:12297624
Page seeded by OCA on Thu Feb 21 13:37:00 2008
