2eyu: Difference between revisions

Revision as of 04:24, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2eyu.png

Template:STRUCTURE 2eyu

The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilTThe Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT

Template:ABSTRACT PUBMED 17355871

About this StructureAbout this Structure

2EYU 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

The pilus-retraction protein PilT: ultrastructure of the biological assembly., Forest KT, Satyshur KA, Worzalla GA, Hansen JK, Herdendorf TJ, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):978-82. Epub 2004, Apr 21. PMID:15103158

Page seeded by OCA on Mon Jul 28 04:23:55 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2eyu.jpg|left|200px]]
+{{Seed}}
+[[Image:2eyu.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2eyu|  PDB=2eyu  |  SCENE=  }}
-'''The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT'''
+===The Crystal Structure of the C-terminal Domain of Aquifex aeolicus PilT===
-==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.
+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.
+-->
+{{ABSTRACT_PUBMED_17355871}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==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://www.ncbi.nlm.nih.gov/pubmed/17355871 17355871]
+The pilus-retraction protein PilT: ultrastructure of the biological assembly., Forest KT, Satyshur KA, Worzalla GA, Hansen JK, Herdendorf TJ, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):978-82. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103158 15103158]
 [[Category: Aquifex aeolicus]]
 [[Category: Single protein]]
@@ Line 30: / Line 36: @@
 [[Category: C-terminal domain pilt]]
 [[Category: Pilus retraction motor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:15:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:23:55 2008''