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| | ==Crystal Structure of nucleotide-free Myosin 1b residues 1-728 with bound Calmodulin== | | ==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=''> | + | <StructureSection load='4l79' size='340' side='right'caption='[[4l79]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[4l79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4L79 FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=4l79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l79 OCA], [https://pdbe.org/4l79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l79 RCSB], [https://www.ebi.ac.uk/pdbsum/4l79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l79 ProSAT]</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> | | </table> |
| | == Function == | | == 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). | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Calmodulin|Calmodulin]] | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] |
| - | *[[Myosin|Myosin]] | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Dominguez, R]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Ostap, E M]] | + | [[Category: Dominguez R]] |
| - | [[Category: Shuman, H]] | + | [[Category: Ostap EM]] |
| - | [[Category: Zwolak, A]] | + | [[Category: Shuman H]] |
| - | [[Category: Actin binding]]
| + | [[Category: Zwolak A]] |
| - | [[Category: Ca2+ binding]]
| + | |
| - | [[Category: Cargo]]
| + | |
| - | [[Category: Membrane binding]]
| + | |
| - | [[Category: Motor protein-metal binding protein complex]]
| + | |
| - | [[Category: Myosin motor]]
| + | |
| - | [[Category: Nucleotide hydrolysis]]
| + | |
| Structural highlights
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.
See Also
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
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