3MJX

Crystal structure of myosin-2 motor domain in complex with ADP-Metavanadate and blebbistatin

Summary for 3MJX

• Entry DOI: 10.2210/pdb3mjx/pdb
• Related: 1YV3 2JHR 2JJ9 3BZ7 3BZ8 3BZ9
• Descriptor: Myosin-2 heavy chain, ADP METAVANADATE, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: contractile protein, allosteric, methylation, atp-binding, motor protein, actin-binding, phosphoprotein, adp-metavanadate, calmodulin-binding, nucleotide-binding, blebbistatin, myosin, structural protein
• Biological source: Dictyostelium discoideum (Slime mold)
• Cellular location: Cytoplasm, cell cortex: P08799
• Total number of polymer chains: 1
• Total formula weight: 90858.35

Authors

Fedorov, R.,Baruch, P.,Bauer, S.,Manstein, D.J. (deposition date: 2010-04-13, release date: 2011-04-27, Last modification date: 2024-03-13)

Primary citation

Fedorov, R.,Bohl, M.,Tsiavaliaris, G.,Hartmann, F.K.,Taft, M.H.,Baruch, P.,Brenner, B.,Martin, R.,Knolker, H.J.,Gutzeit, H.O.,Manstein, D.J.
The mechanism of pentabromopseudilin inhibition of myosin motor activity.
Nat.Struct.Mol.Biol., 16:80-88, 2009

PubMed Abstract: We have identified pentabromopseudilin (PBP) as a potent inhibitor of myosin-dependent processes such as isometric tension development and unloaded shortening velocity. PBP-induced reductions in the rate constants for ATP binding, ATP hydrolysis and ADP dissociation extend the time required per myosin ATPase cycle in the absence and presence of actin. Additionally, coupling between the actin and nucleotide binding sites is reduced in the presence of the inhibitor. The selectivity of PBP differs from that observed with other myosin inhibitors. To elucidate the binding mode of PBP, we crystallized the Dictyostelium myosin-2 motor domain in the presence of Mg(2+)-ADP-meta-vanadate and PBP. The electron density for PBP is unambiguous and shows PBP to bind at a previously unknown allosteric site near the tip of the 50-kDa domain, at a distance of 16 A from the nucleotide binding site and 7.5 A away from the blebbistatin binding pocket.

PubMed: 19122661
DOI: 10.1038/nsmb.1542

Experimental method

X-RAY DIFFRACTION (2.2 Å)