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- | [[Image:1g8x.gif|left|200px]] | |
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- | {{Structure
| + | ==STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR== |
- | |PDB= 1g8x |SIZE=350|CAPTION= <scene name='initialview01'>1g8x</scene>, resolution 2.80Å
| + | <StructureSection load='1g8x' size='340' side='right'caption='[[1g8x]], [[Resolution|resolution]] 2.80Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | + | <table><tr><td colspan='2'>[[1g8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G8X FirstGlance]. <br> |
- | |ACTIVITY= | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
- | |GENE= | + | <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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1g8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8x OCA], [https://pdbe.org/1g8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g8x RCSB], [https://www.ebi.ac.uk/pdbsum/1g8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g8x ProSAT]</span></td></tr> |
| + | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/MYS2_DICDI MYS2_DICDI] Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.[https://www.uniprot.org/uniprot/ACTNA_DICDI ACTNA_DICDI] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.<ref>PMID:10411959</ref> <ref>PMID:10413681</ref> <ref>PMID:10704840</ref> <ref>PMID:1732064</ref> <ref>PMID:3956480</ref> <ref>PMID:6746725</ref> <ref>PMID:8486739</ref> <ref>PMID:8937986</ref> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g8/1g8x_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g8x ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR'''
| + | ==See Also== |
- | | + | *[[Actinin 3D structures|Actinin 3D structures]] |
- | | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
- | ==Overview== | + | == References == |
- | Molecular motors move unidirectionally along polymer tracks, producing movement and force in an ATP-dependent fashion. They achieve this by amplifying small conformational changes in the nucleotide-binding region into force-generating movements of larger protein domains. We present the 2.8 A resolution crystal structure of an artificial actin-based motor. By combining the catalytic domain of myosin II with a 130 A conformational amplifier consisting of repeats 1 and 2 of alpha-actinin, we demonstrate that it is possible to genetically engineer single-polypeptide molecular motors with precisely defined lever arm lengths and specific motile properties. Furthermore, our structure shows the consequences of mutating a conserved salt bridge in the nucleotide-binding region. Disruption of this salt bridge, which is known to severely inhibit ATP hydrolysis activity, appears to interfere with formation of myosin's catalytically active 'closed' conformation. Finally, we describe the structure of alpha-actinin repeats 1 and 2 as being composed of two rigid, triple-helical bundles linked by an uninterrupted alpha-helix. This fold is very similar to the previously described structures of alpha-actinin repeats 2 and 3, and alpha-spectrin repeats 16 and 17.
| + | <references/> |
- | | + | __TOC__ |
- | ==About this Structure==
| + | </StructureSection> |
- | 1G8X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8X OCA].
| + | |
- | | + | |
- | ==Reference== | + | |
- | Structure of a genetically engineered molecular motor., Kliche W, Fujita-Becker S, Kollmar M, Manstein DJ, Kull FJ, EMBO J. 2001 Jan 15;20(1-2):40-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11226153 11226153]
| + | |
| [[Category: Dictyostelium discoideum]] | | [[Category: Dictyostelium discoideum]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Fujita-Becker, S.]] | + | [[Category: Fujita-Becker S]] |
- | [[Category: Kliche, W.]] | + | [[Category: Kliche W]] |
- | [[Category: Kollmar, M.]] | + | [[Category: Kollmar M]] |
- | [[Category: Kull, F J.]] | + | [[Category: Kull FJ]] |
- | [[Category: Manstein, D J.]] | + | [[Category: Manstein DJ]] |
- | [[Category: ADP]]
| + | |
- | [[Category: MG]]
| + | |
- | [[Category: alpha-actinin]]
| + | |
- | [[Category: dictyostelium]]
| + | |
- | [[Category: lever arm]]
| + | |
- | [[Category: motor]]
| + | |
- | [[Category: myosin]]
| + | |
- | [[Category: protein engineering]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:54:02 2008''
| + | |
| Structural highlights
Function
MYS2_DICDI Myosin is a protein that binds to actin and has ATPase activity that is activated by actin.ACTNA_DICDI F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.[1] [2] [3] [4] [5] [6] [7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Weber I. Computer-assisted morphometry of cell-substratum contacts. Croat Med J. 1999 Sep;40(3):334-9. PMID:10411959
- ↑ Rivero F, Furukawa R, Fechheimer M, Noegel AA. Three actin cross-linking proteins, the 34 kDa actin-bundling protein, alpha-actinin and gelation factor (ABP-120), have both unique and redundant roles in the growth and development of Dictyostelium. J Cell Sci. 1999 Aug;112 ( Pt 16):2737-51. PMID:10413681
- ↑ Ponte E, Rivero F, Fechheimer M, Noegel A, Bozzaro S. Severe developmental defects in Dictyostelium null mutants for actin-binding proteins. Mech Dev. 2000 Mar 1;91(1-2):153-61. doi: 10.1016/s0925-4773(99)00292-0. PMID:10704840 doi:http://dx.doi.org/10.1016/s0925-4773(99)00292-0
- ↑ Witke W, Schleicher M, Noegel AA. Redundancy in the microfilament system: abnormal development of Dictyostelium cells lacking two F-actin cross-linking proteins. Cell. 1992 Jan 10;68(1):53-62. PMID:1732064
- ↑ Wallraff E, Schleicher M, Modersitzki M, Rieger D, Isenberg G, Gerisch G. Selection of Dictyostelium mutants defective in cytoskeletal proteins: use of an antibody that binds to the ends of alpha-actinin rods. EMBO J. 1986 Jan;5(1):61-7. PMID:3956480
- ↑ Condeelis J, Vahey M, Carboni JM, DeMey J, Ogihara S. Properties of the 120,000- and 95,000-dalton actin-binding proteins from Dictyostelium discoideum and their possible functions in assembling the cytoplasmic matrix. J Cell Biol. 1984 Jul;99(1 Pt 2):119s-126s. PMID:6746725
- ↑ Witke W, Hofmann A, Koppel B, Schleicher M, Noegel AA. The Ca(2+)-binding domains in non-muscle type alpha-actinin: biochemical and genetic analysis. J Cell Biol. 1993 May;121(3):599-606. PMID:8486739
- ↑ Rivero F, Koppel B, Peracino B, Bozzaro S, Siegert F, Weijer CJ, Schleicher M, Albrecht R, Noegel AA. The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J Cell Sci. 1996 Nov;109 ( Pt 11):2679-91. PMID:8937986
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