2eww: Difference between revisions
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[[Image:2eww.jpg|left|200px]] | [[Image:2eww.jpg|left|200px]] | ||
'''Crystal Structure of the Pilus Retraction Motor PilT and Bound ATP''' | {{Structure | ||
|PDB= 2eww |SIZE=350|CAPTION= <scene name='initialview01'>2eww</scene>, resolution 3.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the Pilus Retraction Motor PilT and Bound ATP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2EWW is a [ | 2EWW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EWW OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17355871 17355871] | ||
[[Category: Aquifex aeolicus]] | [[Category: Aquifex aeolicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pilus retraction motor]] | [[Category: pilus retraction motor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:23 2008'' | ||
Revision as of 17:45, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Pilus Retraction Motor PilT and Bound ATP
OverviewOverview
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 StructureAbout this Structure
2EWW is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
ReferenceReference
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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