2jj9 is a 1 chain structure with sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The mechanism of pentabromopseudilin inhibition of myosin motor activity.,Fedorov R, Bohl M, Tsiavaliaris G, Hartmann FK, Taft MH, Baruch P, Brenner B, Martin R, Knolker HJ, Gutzeit HO, Manstein DJ Nat Struct Mol Biol. 2009 Jan;16(1):80-8. Epub 2009 Jan 4. PMID:19122661[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
