4l79
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin== | |
| - | + | <StructureSection load='4l79' size='340' side='right' caption='[[4l79]], [[Resolution|resolution]] 2.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4l79]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L79 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Myo1a, Myo1b, Myr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), CALM, CALM1, CALM2, CALM3, CALML2, calmodulin, CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l79 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l79 RCSB], [http://www.ebi.ac.uk/pdbsum/4l79 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/MYO1B_RAT MYO1B_RAT]] Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport (By similarity). | [[http://www.uniprot.org/uniprot/MYO1B_RAT MYO1B_RAT]] Motor protein that may participate in process critical to neuronal development and function such as cell migration, neurite outgrowth and vesicular transport (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Myosins are molecular motors that power diverse cellular processes, such as rapid organelle transport, muscle contraction, and tension-sensitive anchoring. The structural adaptations in the motor that allow for this functional diversity are not known, due, in part, to the lack of high-resolution structures of highly tension-sensitive myosins. We determined a 2.3-A resolution structure of apo-myosin-Ib (Myo1b), which is the most tension-sensitive myosin characterized. We identified a striking unique orientation of structural elements that position the motor's lever arm. This orientation results in a cavity between the motor and lever arm that holds a 10-residue stretch of N-terminal amino acids, a region that is divergent among myosins. Single-molecule and biochemical analyses show that the N terminus plays an important role in stabilizing the post power-stroke conformation of Myo1b and in tuning the rate of the force-sensitive transition. We propose that this region plays a general role in tuning the mechanochemical properties of myosins. | ||
| - | + | A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.,Shuman H, Greenberg MJ, Zwolak A, Lin T, Sindelar CV, Dominguez R, Ostap EM Proc Natl Acad Sci U S A. 2014 Feb 11;111(6):2116-21. doi:, 10.1073/pnas.1321022111. Epub 2014 Jan 27. PMID:24469830<ref>PMID:24469830</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Calmodulin|Calmodulin]] | *[[Calmodulin|Calmodulin]] | ||
| - | + | *[[Myosin|Myosin]] | |
| - | == | + | == References == |
| - | + | <references/> | |
| - | [[Category: Dominguez, R | + | __TOC__ |
| - | [[Category: Ostap, E M | + | </StructureSection> |
| - | [[Category: Shuman, H | + | [[Category: Buffalo rat]] |
| - | [[Category: Zwolak, A | + | [[Category: Human]] |
| + | [[Category: Dominguez, R]] | ||
| + | [[Category: Ostap, E M]] | ||
| + | [[Category: Shuman, H]] | ||
| + | [[Category: Zwolak, A]] | ||
[[Category: Actin binding]] | [[Category: Actin binding]] | ||
[[Category: Ca2+ binding]] | [[Category: Ca2+ binding]] | ||
Revision as of 17:53, 25 December 2014
Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin
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