2ewv: Difference between revisions

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==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.

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==

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[[Category: Aquifex aeolicus vf5]]

[[Category: Single protein]]

[[Category: Forest, K.T.]]

[[Category: Forest, K T.]]

[[Category: Satyshur, K.A.]]

[[Category: Satyshur, K A.]]

[[Category: ADP]]

[[Category: atpase]]

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[[Category: pilus retraction motor]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Aquifex aeolicus vf5]]
 [[Category: Single protein]]
-[[Category: Forest, K.T.]]
+[[Category: Forest, K T.]]
-[[Category: Satyshur, K.A.]]
+[[Category: Satyshur, K A.]]
 [[Category: ADP]]
 [[Category: atpase]]
@@ Line 20: / Line 20: @@
 [[Category: pilus retraction motor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:55:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:23 2008''