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.


2e5t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2e5t.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2e5t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2e5t| PDB=2e5t | SCENE= }}
{{STRUCTURE_2e5t| PDB=2e5t | SCENE= }}
-
'''C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP condition'''
+
===C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP condition===
-
==Overview==
+
<!--
-
The epsilon subunit of bacterial and chloroplast F(o)F(1)-ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound epsilon subunit from a thermophilic Bacillus PS3 at 1.9-A resolution. The C-terminal two alpha-helices were folded into a hairpin, sitting on the beta sandwich structure, as reported for Escherichia coli. A previously undescribed ATP binding motif, I(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli epsilon subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 epsilon subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the epsilon C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of F(o)F(1)-ATP synthase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17581881}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17581881 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17581881}}
==About this Structure==
==About this Structure==
-
2E5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._ps3 Bacillus sp. ps3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5T OCA].
+
2E5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp._ps3 Bacillus sp. ps3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5T OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: F1-atpase]]
[[Category: F1-atpase]]
[[Category: F1fo atp synthase]]
[[Category: F1fo atp synthase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:58:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:59:19 2008''

Revision as of 12:59, 29 July 2008

Image:2e5t.png

Template:STRUCTURE 2e5t

C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic bacillus PS3 in the presence of ATP condition

Template:ABSTRACT PUBMED 17581881

About this Structure

2E5T is a Single protein structure of sequence from Bacillus sp. ps3. Full experimental information is available from OCA.

Reference

Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1., Yagi H, Kajiwara N, Tanaka H, Tsukihara T, Kato-Yamada Y, Yoshida M, Akutsu H, Proc Natl Acad Sci U S A. 2007 Jul 3;104(27):11233-8. Epub 2007 Jun 20. PMID:17581881

Page seeded by OCA on Tue Jul 29 15:59:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2e5t"
Personal tools