2gsz

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{{STRUCTURE_2gsz| PDB=2gsz | SCENE= }}
{{STRUCTURE_2gsz| PDB=2gsz | SCENE= }}
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'''Structure of A. aeolicus PilT with 6 monomers per asymmetric unit'''
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===Structure of A. aeolicus PilT with 6 monomers per asymmetric unit===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17355871 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17355871}}
==About this Structure==
==About this Structure==
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[[Category: Pa]]
[[Category: Pa]]
[[Category: Reca]]
[[Category: Reca]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:29:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:40:57 2008''

Revision as of 00:41, 28 July 2008

Template:STRUCTURE 2gsz

Structure of A. aeolicus PilT with 6 monomers per asymmetric unit

Template:ABSTRACT PUBMED 17355871

About this Structure

2GSZ 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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