2Y0R

Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2

Summary for 2Y0R

• Entry DOI: 10.2210/pdb2y0r/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 2JJ9 2X9H 2XEL 2XO8 2Y8I 2Y9E
• Descriptor: MYOSIN-2 HEAVY CHAIN (2 entities in total)
• Functional Keywords: motor protein
• Biological source: DICTYOSTELIUM DISCOIDEUM
• Total number of polymer chains: 1
• Total formula weight: 86379.70

Authors

Preller, M.,Bauer, S.,Adamek, N.,Fujita-Becker, S.,Fedorov, R.,Geeves, M.A.,Manstein, D.J. (deposition date: 2010-12-07, release date: 2011-07-20, Last modification date: 2023-12-20)

Primary citation

Preller, M.,Bauer, S.,Adamek, N.,Fujita-Becker, S.,Fedorov, R.,Geeves, M.A.,Manstein, D.J.
Structural Basis for the Allosteric Interference of Myosin Function by Reactive Thiol Region Mutations G680A and G680V.
J.Biol.Chem., 286:35051-, 2011

PubMed Abstract: The cold-sensitive single-residue mutation of glycine 680 in the reactive thiol region of Dictyostelium discoideum myosin-2 or the corresponding conserved glycine in other myosin isoforms has been reported to interfere with motor function. Here we present the x-ray structures of myosin motor domain mutants G680A in the absence and presence of nucleotide as well as the apo structure of mutant G680V. Our results show that the Gly-680 mutations lead to uncoupling of the reactive thiol region from the surrounding structural elements. Structural and functional data indicate that the mutations induce the preferential population of a state that resembles the ADP-bound state. Moreover, the Gly-680 mutants display greatly reduced dynamic properties, which appear to be related to the recovery of myosin motor function at elevated temperatures.

PubMed: 21841195
DOI: 10.1074/JBC.M111.265298

Experimental method

X-RAY DIFFRACTION (2.85 Å)