1g8x

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|PDB= 1g8x |SIZE=350|CAPTION= <scene name='initialview01'>1g8x</scene>, resolution 2.80&Aring;
|PDB= 1g8x |SIZE=350|CAPTION= <scene name='initialview01'>1g8x</scene>, resolution 2.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g8x OCA], [http://www.ebi.ac.uk/pdbsum/1g8x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g8x RCSB]</span>
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}}
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[[Category: Kull, F J.]]
[[Category: Kull, F J.]]
[[Category: Manstein, D J.]]
[[Category: Manstein, D J.]]
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[[Category: ADP]]
 
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[[Category: MG]]
 
[[Category: alpha-actinin]]
[[Category: alpha-actinin]]
[[Category: dictyostelium]]
[[Category: dictyostelium]]
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[[Category: protein engineering]]
[[Category: protein engineering]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:54:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:06 2008''

Revision as of 17:39, 30 March 2008


PDB ID 1g8x

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR


Overview

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.

About this Structure

1G8X is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from 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:11226153

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