Structural highlights
2x51 is a 2 chain structure with sequence from Drome and Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Related: | 2v26, 2vas, 2bbm, 4cln, 1mxe, 2bkh, 2vb6, 2bki, 2bbn, 3l9i |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[MYO6_PIG] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).[1] [CALM_DROME] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Publication Abstract from PubMed
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.
Role of Insert-1 of Myosin VI in Modulating Nucleotide Affinity.,Pylypenko O, Song L, Squires G, Liu X, Zong AB, Houdusse A, Sweeney HL J Biol Chem. 2011 Apr 1;286(13):11716-23. Epub 2011 Jan 29. PMID:21278381[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Naccache SN, Hasson T. Myosin VI altered at threonine 406 stabilizes actin filaments in vivo. Cell Motil Cytoskeleton. 2006 Oct;63(10):633-45. PMID:16917816 doi:http://dx.doi.org/10.1002/cm.20150
- ↑ Pylypenko O, Song L, Squires G, Liu X, Zong AB, Houdusse A, Sweeney HL. Role of Insert-1 of Myosin VI in Modulating Nucleotide Affinity. J Biol Chem. 2011 Apr 1;286(13):11716-23. Epub 2011 Jan 29. PMID:21278381 doi:10.1074/jbc.M110.200626
