1br2

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Revision as of 09:43, 20 November 2007

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spinqualitylabelsall models 1br2, resolution 2.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 MG, ALF and ADP 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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