1M45
CRYSTAL STRUCTURE OF MLC1P BOUND TO IQ2 OF MYO2P, A CLASS V MYOSIN
Summary for 1M45
| Entry DOI | 10.2210/pdb1m45/pdb |
| Related | 1M46 |
| Descriptor | Myosin light chain, IQ2 Motif from MYO2P, A Class V Myosin (3 entities in total) |
| Functional Keywords | protein-peptide complex, iq motif, myosin light chain, cell cycle protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Bud neck: P53141 P19524 |
| Total number of polymer chains | 2 |
| Total formula weight | 19325.63 |
| Authors | Terrak, M.,Dominguez, R. (deposition date: 2002-07-02, release date: 2003-02-11, Last modification date: 2024-02-14) |
| Primary citation | Terrak, M.,Wu, G.,Stafford, W.F.,Lu, R.C.,Dominguez, R. Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications Embo J., 22:362-371, 2003 Cited by PubMed Abstract: IQ motifs are widespread in nature. Mlc1p is a calmodulin-like myosin light chain that binds to IQ motifs of a class V myosin, Myo2p, and an IQGAP-related protein, Iqg1p, playing a role in polarized growth and cytokinesis in Saccharomyces cerevisiae. The crystal structures of Mlc1p bound to IQ2 and IQ4 of Myo2p differ dramatically. When bound to IQ2, Mlc1p adopts a compact conformation in which both the N- and C-lobes interact with the IQ motif. However, in the complex with IQ4, the N-lobe no longer interacts with the IQ motif, resulting in an extended conformation of Mlc1p. The two light chain structures relate to two distinct subfamilies of IQ motifs, one of which does not interact with the N-lobes of calmodulin-like light chains. The correlation between light chain structure and IQ sequence is demonstrated further by sedimentation velocity analysis of complexes of Mlc1p with IQ motifs from Myo2p and Iqg1p. The resulting 'free' N-lobes of myosin light chains in the extended conformation could mediate the formation of ternary complexes during protein localization and/or partner recruitment. PubMed: 12554638DOI: 10.1093/emboj/cdg058 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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