1nwk
From Proteopedia
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|PDB= 1nwk |SIZE=350|CAPTION= <scene name='initialview01'>1nwk</scene>, resolution 1.85Å | |PDB= 1nwk |SIZE=350|CAPTION= <scene name='initialview01'>1nwk</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1j6z|1J6Z]] | ||
| + | |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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[[Category: Dominguez, R.]] | [[Category: Dominguez, R.]] | ||
[[Category: Graceffa, P.]] | [[Category: Graceffa, P.]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: RHO]] | ||
[[Category: actin]] | [[Category: actin]] | ||
[[Category: amppnp]] | [[Category: amppnp]] | ||
| Line 32: | Line 32: | ||
[[Category: tetramethylrhodamine-5-maleimide]] | [[Category: tetramethylrhodamine-5-maleimide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:29 2008'' |
Revision as of 19:36, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1J6Z
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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