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| [[Image:2gsz.jpg|left|200px]] | | {{Seed}} |
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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'''
| | ===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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17355871}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17355871 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17355871}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pa]] | | [[Category: Pa]] |
| [[Category: Reca]] | | [[Category: Reca]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:29:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:40:57 2008'' |
