1br1

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Revision as of 06:50, 18 November 2007

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spinqualitylabelsall models 1br1, resolution 3.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.ALF4 BOUND AT THE ACTIVE SITE

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

1BR1 is a Protein complex structure of sequences from Gallus gallus with MG, ALF and ADP as ligands. The following page contains interesting information on the relation of 1BR1 with [Myosin]. 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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