1nwk

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[[Image:1nwk.gif|left|200px]]
[[Image:1nwk.gif|left|200px]]
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{{Structure
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|PDB= 1nwk |SIZE=350|CAPTION= <scene name='initialview01'>1nwk</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_1nwk", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=RHO:TETRAMETHYLRHODAMINE-5-MALEIMIDE'>RHO</scene>
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{{STRUCTURE_1nwk| PDB=1nwk | SCENE= }}
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|RELATEDENTRY=[[1j6z|1J6Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nwk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nwk OCA], [http://www.ebi.ac.uk/pdbsum/1nwk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nwk RCSB]</span>
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'''CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE'''
'''CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE'''
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[[Category: Dominguez, R.]]
[[Category: Dominguez, R.]]
[[Category: Graceffa, P.]]
[[Category: Graceffa, P.]]
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[[Category: actin]]
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[[Category: Actin]]
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[[Category: amppnp]]
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[[Category: Amppnp]]
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[[Category: atp-state]]
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[[Category: Atp-state]]
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[[Category: tetramethylrhodamine-5-maleimide]]
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[[Category: Tetramethylrhodamine-5-maleimide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:03:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:29 2008''
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Revision as of 00:03, 3 May 2008

Image:1nwk.gif

Template:STRUCTURE 1nwk

CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE


Overview

A nucleotide-dependent conformational change regulates actin filament dynamics. Yet, the structural basis of this mechanism remains controversial. The x-ray crystal structure of tetramethylrhodamine-5-maleimide-actin with bound AMPPNP, a non-hydrolyzable ATP analog, was determined to 1.85-A resolution. A comparison of this structure to that of tetramethylrhodamine-5-maleimide-actin with bound ADP, determined previously under similar conditions, reveals how the release of the nucleotide gamma-phosphate sets in motion a sequence of events leading to a conformational change in subdomain 2. The side chain of Ser-14 in the catalytic site rotates upon Pi release, triggering the rearrangement of the loop containing the methylated His-73, referred to as the sensor loop. This in turn causes a transition in the DNase I-binding loop in subdomain 2 from a disordered loop in ATP-actin to an ordered alpha-helix in ADP-actin. Despite this conformational change, the nucleotide cleft remains closed in ADP-actin, similar to ATP-actin. An analysis of the existing structures of members of the actin superfamily suggests that the cleft is open in the nucleotide-free state.

About this Structure

1NWK is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics., Graceffa P, Dominguez R, J Biol Chem. 2003 Sep 5;278(36):34172-80. Epub 2003 Jun 17. PMID:12813032 Page seeded by OCA on Sat May 3 03:03:54 2008

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