This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ny5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ny5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ny5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ny5| PDB=1ny5 | SCENE= }}
{{STRUCTURE_1ny5| PDB=1ny5 | SCENE= }}
-
'''Crystal structure of sigm54 activator (AAA+ ATPase) in the inactive state'''
+
===Crystal structure of sigm54 activator (AAA+ ATPase) in the inactive state===
-
==Overview==
+
<!--
-
Transcription by sigma54 RNA polymerase depends on activators that contain ATPase domains of the AAA+ class. These activators, which are often response regulators of two-component signal transduction systems, remodel the polymerase so that it can form open complexes at promoters. Here, we report the first crystal structures of the ATPase domain of an activator, the NtrC1 protein from the extreme thermophile Aquifex aeolicus. This domain alone, which is active, crystallized as a ring-shaped heptamer. The protein carrying both the ATPase and adjacent receiver domains, which is inactive, crystallized as a dimer. In the inactive dimer, one residue needed for catalysis is far from the active site, and extensive contacts among the domains prevent oligomerization of the ATPase domain. Oligomerization, which completes the active site, depends on surfaces that are buried in the dimer, and hence, on a rearrangement of the receiver domains upon phosphorylation. A motif in the ATPase domain known to be critical for coupling energy to remodeling of polymerase forms a novel loop that projects from the middle of an alpha helix. The extended, structured loops from the subunits of the heptamer localize to a pore in the center of the ring and form a surface that could contact sigma54.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14561776}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14561776 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14561776}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Dimer]]
[[Category: Dimer]]
[[Category: Sigma54 activator]]
[[Category: Sigma54 activator]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:07:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:46:51 2008''

Revision as of 13:46, 27 July 2008

Image:1ny5.png

Template:STRUCTURE 1ny5

Crystal structure of sigm54 activator (AAA+ ATPase) in the inactive state

Template:ABSTRACT PUBMED 14561776

About this Structure

1NY5 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains., Lee SY, De La Torre A, Yan D, Kustu S, Nixon BT, Wemmer DE, Genes Dev. 2003 Oct 15;17(20):2552-63. PMID:14561776

Page seeded by OCA on Sun Jul 27 16:46:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ny5"
Personal tools