2fcd: Difference between revisions

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[[Image:2fcd.gif|left|200px]]
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[[Image:2fcd.png|left|200px]]


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{{STRUCTURE_2fcd|  PDB=2fcd  |  SCENE=  }}  
{{STRUCTURE_2fcd|  PDB=2fcd  |  SCENE=  }}  


'''Solution structure of N-lobe Myosin Light Chain from Saccharomices cerevisiae'''
===Solution structure of N-lobe Myosin Light Chain from Saccharomices cerevisiae===




==Overview==
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Calmodulin, regulatory, and essential myosin light chain are evolutionary conserved proteins that, by binding to IQ motifs of target proteins, regulate essential intracellular processes among which are efficiency of secretory vesicles release at synapsis, intracellular signaling, and regulation of cell division. The yeast Saccharomyces cerevisiae calmodulin Cmd1 and the essential myosin light chain Mlc1p share the ability to interact with the class V myosin Myo2p and Myo4 and the class II myosin Myo1p. These myosins are required for vesicle, organelle, and mRNA transport, spindle orientation, and cytokinesis. We have used the budding yeast model system to study how calmodulin and essential myosin light chain selectively regulate class V myosin function. NMR structural analysis of uncomplexed Mlc1p and interaction studies with the first three IQ motifs of Myo2p show that the structural similarities between Mlc1p and the other members of the EF-hand superfamily of calmodulin-like proteins are mainly restricted to the C-lobe of these proteins. The N-lobe of Mlc1p presents a significantly compact and stable structure that is maintained both in the free and complexed states. The Mlc1p N-lobe interacts with the IQ motif in a manner that is regulated both by the IQ motifs sequence as well as by light chain structural features. These characteristic allows a distinctive interaction of Mlc1p with the first IQ motif of Myo2p when compared with calmodulin. This finding gives us a novel view of how calmodulin and essential light chain, through a differential binding to IQ1 of class V myosin motor, regulate this activity during vegetative growth and cytokinesis.
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==About this Structure==
==About this Structure==
2FCD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCD OCA].  
2FCD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCD OCA].  


==Reference==
==Reference==
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[[Category: Ragnini-Wilson, A.]]
[[Category: Ragnini-Wilson, A.]]
[[Category: Ef-hand protein]]
[[Category: Ef-hand protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:43:38 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:00:13 2008''

Revision as of 17:00, 28 July 2008

File:2fcd.png

Template:STRUCTURE 2fcd

Solution structure of N-lobe Myosin Light Chain from Saccharomices cerevisiae

Template:ABSTRACT PUBMED 17074768

About this Structure

2FCD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

Structural basis for the interaction of the myosin light chain Mlc1p with the myosin V Myo2p IQ motifs., Pennestri M, Melino S, Contessa GM, Casavola EC, Paci M, Ragnini-Wilson A, Cicero DO, J Biol Chem. 2007 Jan 5;282(1):667-79. Epub 2006 Oct 29. PMID:17074768

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