2eww
From Proteopedia
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|PDB= 2eww |SIZE=350|CAPTION= <scene name='initialview01'>2eww</scene>, resolution 3.20Å | |PDB= 2eww |SIZE=350|CAPTION= <scene name='initialview01'>2eww</scene>, resolution 3.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eww OCA], [http://www.ebi.ac.uk/pdbsum/2eww PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eww RCSB]</span> | ||
}} | }} | ||
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[[Category: Forest, K T.]] | [[Category: Forest, K T.]] | ||
[[Category: Satyshur, K A.]] | [[Category: Satyshur, K A.]] | ||
| - | [[Category: ATP]] | ||
[[Category: atpase]] | [[Category: atpase]] | ||
[[Category: hexameric pilt]] | [[Category: hexameric pilt]] | ||
[[Category: pilus retraction motor]] | [[Category: pilus retraction motor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:54:52 2008'' |
Revision as of 23:54, 30 March 2008
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| , resolution 3.20Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Pilus Retraction Motor PilT and Bound ATP
Overview
PilT is a hexameric ATPase required for bacterial type IV pilus retraction and surface motility. Crystal structures of ADP- and ATP-bound Aquifex aeolicus PilT at 2.8 and 3.2 A resolution show N-terminal PAS-like and C-terminal RecA-like ATPase domains followed by a set of short C-terminal helices. The hexamer is formed by extensive polar subunit interactions between the ATPase core of one monomer and the N-terminal domain of the next. An additional structure captures a nonsymmetric PilT hexamer in which approach of invariant arginines from two subunits to the bound nucleotide forms an enzymatically competent active site. A panel of pilT mutations highlights the importance of the arginines, the PAS-like domain, the polar subunit interface, and the C-terminal helices for retraction. We present a model for ATP binding leading to dramatic PilT domain motions, engagement of the arginine wire, and subunit communication in this hexameric motor. Our conclusions apply to the entire type II/IV secretion ATPase family.
About this Structure
2EWW is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility., Satyshur KA, Worzalla GA, Meyer LS, Heiniger EK, Aukema KG, Misic AM, Forest KT, Structure. 2007 Mar;15(3):363-76. PMID:17355871
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