1BR1

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

Summary for 1BR1

• Entry DOI: 10.2210/pdb1br1/pdb
• Descriptor: MYOSIN, MAGNESIUM ION, TETRAFLUOROALUMINATE ION, ... (6 entities in total)
• Functional Keywords: muscle protein
• Biological source: Gallus gallus (chicken); More
• Cellular location: Cytoplasm, myofibril: P10587
• Total number of polymer chains: 8
• Total formula weight: 444498.74

Authors

Dominguez, R.,Trybus, K.M.,Cohen, C. (deposition date: 1998-08-26, release date: 1998-09-09, Last modification date: 2024-04-03)

Primary citation

Dominguez, R.,Freyzon, Y.,Trybus, K.M.,Cohen, C.
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.
Cell(Cambridge,Mass.), 94:559-571, 1998

PubMed Abstract: 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.

PubMed: 9741621
DOI: 10.1016/S0092-8674(00)81598-6

Experimental method

X-RAY DIFFRACTION (3.5 Å)