2JJ9
Crystal structure of myosin-2 in complex with ADP-metavanadate
Summary for 2JJ9
| Entry DOI | 10.2210/pdb2jj9/pdb |
| Related | 1D0X 1D0Y 1D0Z 1D1A 1D1B 1D1C 1FMV 1FMW 1G8X 1JWY 1JX2 1LVK 1MMA 1MMD 1MMG 1MMN 1MND 1MNE 1Q5G 1VOM 1W9I 1W9J 1W9K 1W9L 1YV3 2AKA 2JHR |
| Descriptor | MYOSIN-2 HEAVY CHAIN, ADP METAVANADATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | calmodulin-binding, nucleotide-binding, motor protein, actin-binding, phosphoprotein, myosin, cytoplasm, atp-analog, methylation, coiled coil, atp-binding, motor-domain, contractile protein |
| Biological source | DICTYOSTELIUM DISCOIDEUM (SLIME MOLD) |
| Total number of polymer chains | 1 |
| Total formula weight | 90566.02 |
| Authors | Fedorov, R.,Boehl, M.,Tsiavaliaris, G.,Hartmann, F.K.,Baruch, P.,Brenner, B.,Martin, R.,Knoelker, H.J.,Gutzeit, H.O.,Manstein, D.J. (deposition date: 2008-03-25, release date: 2009-01-13, Last modification date: 2023-12-13) |
| Primary citation | Fedorov, R.,Bohl, M.,Tsiavaliaris, G.,Hartmann, F.K.,Taft, M.H.,Baruch, P.,Brenner, B.,Martin, R.,Knolker, H.,Gutzeit, H.O.,Manstein, D.J. The Mechanism of Pentabromopseudilin Inhibition of Myosin Motor Activity. Nat.Struct.Mol.Biol., 16:80-, 2009 Cited by 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: 19122661DOI: 10.1038/NSMB.1542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
