1fmw
From Proteopedia
(New page: 200px<br /><applet load="1fmw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmw, resolution 2.15Å" /> '''CRYSTAL STRUCTURE OF...) |
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- | [[Image:1fmw.jpg|left|200px]]<br /><applet load="1fmw" size=" | + | [[Image:1fmw.jpg|left|200px]]<br /><applet load="1fmw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fmw, resolution 2.15Å" /> | caption="1fmw, resolution 2.15Å" /> | ||
'''CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II'''<br /> | '''CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II'''<br /> | ||
==Overview== | ==Overview== | ||
- | Myosin is the most comprehensively studied molecular motor that converts | + | Myosin is the most comprehensively studied molecular motor that converts energy from the hydrolysis of MgATP into directed movement. Its motile cycle consists of a sequential series of interactions between myosin, actin, MgATP, and the products of hydrolysis, where the affinity of myosin for actin is modulated by the nature of the nucleotide bound in the active site. The first step in the contractile cycle occurs when ATP binds to actomyosin and releases myosin from the complex. We report here the structure of the motor domain of Dictyostelium discoideum myosin II both in its nucleotide-free state and complexed with MgATP. The structure with MgATP was obtained by soaking the crystals in substrate. These structures reveal that both the apo form and the MgATP complex are very similar to those previously seen with MgATPgammaS and MgAMP-PNP. Moreover, these structures are similar to that of chicken skeletal myosin subfragment-1. The crystallized protein is enzymatically active in solution, indicating that the conformation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most likely represents the pre-hydrolysis structure for the myosin head that occurs after release from actin. |
==About this Structure== | ==About this Structure== | ||
- | 1FMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Bauer, C | + | [[Category: Bauer, C B.]] |
- | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: Smith, R.]] | [[Category: Smith, R.]] | ||
- | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: myosin motor domaim]] | [[Category: myosin motor domaim]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:20 2008'' |
Revision as of 10:40, 21 February 2008
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CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAIN OF DICTYOSTELIUM MYOSIN II
Overview
Myosin is the most comprehensively studied molecular motor that converts energy from the hydrolysis of MgATP into directed movement. Its motile cycle consists of a sequential series of interactions between myosin, actin, MgATP, and the products of hydrolysis, where the affinity of myosin for actin is modulated by the nature of the nucleotide bound in the active site. The first step in the contractile cycle occurs when ATP binds to actomyosin and releases myosin from the complex. We report here the structure of the motor domain of Dictyostelium discoideum myosin II both in its nucleotide-free state and complexed with MgATP. The structure with MgATP was obtained by soaking the crystals in substrate. These structures reveal that both the apo form and the MgATP complex are very similar to those previously seen with MgATPgammaS and MgAMP-PNP. Moreover, these structures are similar to that of chicken skeletal myosin subfragment-1. The crystallized protein is enzymatically active in solution, indicating that the conformation of myosin observed in chicken skeletal myosin subfragment-1 is unable to hydrolyze ATP and most likely represents the pre-hydrolysis structure for the myosin head that occurs after release from actin.
About this Structure
1FMW is a Single protein structure of sequence from Dictyostelium discoideum with and as ligands. Full crystallographic information is available from OCA.
Reference
X-ray structures of the apo and MgATP-bound states of Dictyostelium discoideum myosin motor domain., Bauer CB, Holden HM, Thoden JB, Smith R, Rayment I, J Biol Chem. 2000 Dec 8;275(49):38494-9. PMID:10954715
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