|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1w7i' size='340' side='right'caption='[[1w7i]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1w7i' size='340' side='right'caption='[[1w7i]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w7i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1W7I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w7i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W7I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=1w7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7i OCA], [http://pdbe.org/1w7i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1w7i RCSB], [http://www.ebi.ac.uk/pdbsum/1w7i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7i ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=1w7i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w7i OCA], [https://pdbe.org/1w7i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w7i RCSB], [https://www.ebi.ac.uk/pdbsum/1w7i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w7i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYO5A_CHICK MYO5A_CHICK]] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity). | + | [https://www.uniprot.org/uniprot/MYO5A_CHICK MYO5A_CHICK] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Myosin|Myosin]] | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coureux, P D]] | + | [[Category: Coureux P-D]] |
| - | [[Category: Houdusse, A]] | + | [[Category: Houdusse A]] |
| - | [[Category: Sweeney, H L]] | + | [[Category: Sweeney HL]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Chicken]]
| + | |
| - | [[Category: Elc]]
| + | |
| - | [[Category: Iq motif]]
| + | |
| - | [[Category: Mgadp]]
| + | |
| - | [[Category: Molecular motor]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Muscle protein]]
| + | |
| - | [[Category: Myosin v]]
| + | |
| - | [[Category: Unconventional myosin]]
| + | |
| Structural highlights
Function
MYO5A_CHICK Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The molecular motor, myosin, undergoes conformational changes in order to convert chemical energy into force production. Based on kinetic and structural considerations, we assert that three crystal forms of the myosin V motor delineate the conformational changes that myosin motors undergo upon detachment from actin. First, a motor domain structure demonstrates that nucleotide-free myosin V adopts a specific state (rigor-like) that is not influenced by crystal packing. A second structure reveals an actomyosin state that favors rapid release of ADP, and differs from the rigor-like state by a P-loop rearrangement. Comparison of these structures with a third structure, a 2.0 angstroms resolution structure of the motor bound to an ATP analog, illuminates the structural features that provide communication between the actin interface and nucleotide-binding site. Paramount among these is a region we name the transducer, which is composed of the seven-stranded beta-sheet and associated loops and linkers. Reminiscent of the beta-sheet distortion of the F1-ATPase, sequential distortion of this transducer region likely controls sequential release of products from the nucleotide pocket during force generation.
Three myosin V structures delineate essential features of chemo-mechanical transduction.,Coureux PD, Sweeney HL, Houdusse A EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:15510214[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Coureux PD, Sweeney HL, Houdusse A. Three myosin V structures delineate essential features of chemo-mechanical transduction. EMBO J. 2004 Nov 24;23(23):4527-37. Epub 2004 Oct 28. PMID:15510214
|
