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4l79

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Revision as of 10:02, 5 August 2016

Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin

Structural highlights

4l79 is a 2 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Myo1a, Myo1b, Myr1 (Buffalo rat), CALM, CALM1, CALM2, CALM3, CALML2, calmodulin, CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shuman H, Greenberg MJ, Zwolak A, Lin T, Sindelar CV, Dominguez R, Ostap EM. A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning. 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 doi:http://dx.doi.org/10.1073/pnas.1321022111

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4l79"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin==
 <StructureSection load='4l79' size='340' side='right' caption='[[4l79]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
+<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://pdbe.org/4l79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l79 RCSB], [http://www.ebi.ac.uk/pdbsum/4l79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l79 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4l79" style="background-color:#fffaf0;"></div>
 ==See Also==

4l79

From Proteopedia

Revision as of 10:02, 5 August 2016

Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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