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2X51

M6 delta Insert1

Summary for 2X51
Entry DOI10.2210/pdb2x51/pdb
Related1MXE 2BBM 2BBN 2BKH 2BKI 2V26 2VAS 2VB6 3L9I 4CLN
DescriptorMYOSIN-VI, CALMODULIN, GLYCEROL, ... (6 entities in total)
Functional Keywordsmotor protein-signaling protein complex, endocytosis, protein transport, calmodulin-binding, transport, actin-binding, golgi apparatus, motor protein/signaling protein
Biological sourceSUS SCROFA (PIG)
More
Cellular locationGolgi apparatus, trans-Golgi network membrane; Peripheral membrane protein (By similarity): Q29122
Total number of polymer chains2
Total formula weight107717.15
Authors
Squires, G.,Houdusse, A. (deposition date: 2010-02-04, release date: 2011-01-26, Last modification date: 2023-12-20)
Primary citationPylypenko, O.,Song, L.,Squires, G.,Liu, X.,Zong, A.B.,Houdusse, A.,Sweeney, H.L.
Role of Insert-1 of Myosin Vi in Modulating Nucleotide Affinity.
J.Biol.Chem., 286:11716-, 2011
Cited by
PubMed Abstract: Myosin VI is unique in its directionality among myosin superfamily members and also displays a slow and strain-dependent rate of ATP binding that allows for gating between its heads. In this study we demonstrate that leucine 310 is positioned by a class VI-specific insert, insert-1, so as to account for the selective hindrance of ATP versus ADP binding. Mutation of leucine 310 to glycine removes all influence of insert-1 on ATP binding. Furthermore, by analyzing myosin VI structures with either leucine 310 substituted to a glycine or complete removal of insert-1, we conclude that nucleotides may initially bind to myosin by their purine rings before docking their phosphate moieties. Otherwise, insert-1 could not exert a differential influence on ATP versus ADP binding.
PubMed: 21278381
DOI: 10.1074/JBC.M110.200626
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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