1br2

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(New page: 200px<br /><applet load="1br2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1br2, resolution 2.9&Aring;" /> '''SMOOTH MUSCLE MYOSIN ...)
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[[Image:1br2.gif|left|200px]]<br /><applet load="1br2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1br2, resolution 2.9&Aring;" />
caption="1br2, resolution 2.9&Aring;" />
'''SMOOTH MUSCLE MYOSIN MOTOR DOMAIN COMPLEXED WITH MGADP.ALF4'''<br />
'''SMOOTH MUSCLE MYOSIN MOTOR DOMAIN COMPLEXED WITH MGADP.ALF4'''<br />
==Overview==
==Overview==
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The crystal structures of an expressed vertebrate smooth muscle myosin, motor domain (MD) and a motor domain-essential light chain (ELC) complex, (MDE), both with a transition state analog (MgADP x AIF4-) in the active, site, have been determined to 2.9 A and 3.5 A resolution, respectively., The MDE structure with an ATP analog (MgADP x BeFx) was also determined to, 3.6 A resolution. In all three structures, a domain of the C-terminal, region, the "converter," is rotated approximately 70 degrees from that in, nucleotide-free skeletal subfragment 1 (S1). We have found that the, MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with, the fact that they both bind weakly to actin. A comparison of the lever, arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a, potential displacement of approximately 10 nm can be achieved during the, power stroke.
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The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively. The MDE structure with an ATP analog (MgADP x BeFx) was also determined to 3.6 A resolution. In all three structures, a domain of the C-terminal region, the "converter," is rotated approximately 70 degrees from that in nucleotide-free skeletal subfragment 1 (S1). We have found that the MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with the fact that they both bind weakly to actin. A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke.
==About this Structure==
==About this Structure==
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1BR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with MG, ALF and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BR2 OCA].
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1BR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Myosin_ATPase Myosin ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.1 3.6.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BR2 OCA].
==Reference==
==Reference==
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[[Category: Cohen, C.]]
[[Category: Cohen, C.]]
[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
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[[Category: Trybus, K.M.]]
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[[Category: Trybus, K M.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: ALF]]
[[Category: ALF]]
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[[Category: muscle protein]]
[[Category: muscle protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:10 2008''

Revision as of 09:58, 21 February 2008

Image:1br2.gif

1br2, resolution 2.9Å

Drag the structure with the mouse to rotate

SMOOTH MUSCLE MYOSIN MOTOR DOMAIN COMPLEXED WITH MGADP.ALF4

Overview

The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively. The MDE structure with an ATP analog (MgADP x BeFx) was also determined to 3.6 A resolution. In all three structures, a domain of the C-terminal region, the "converter," is rotated approximately 70 degrees from that in nucleotide-free skeletal subfragment 1 (S1). We have found that the MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with the fact that they both bind weakly to actin. A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke.

About this Structure

1BR2 is a Single protein structure of sequence from Gallus gallus with , and as ligands. Active as Myosin ATPase, with EC number 3.6.4.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state., Dominguez R, Freyzon Y, Trybus KM, Cohen C, Cell. 1998 Sep 4;94(5):559-71. PMID:9741621

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