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.


2f3g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2f3g.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2f3g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2f3g| PDB=2f3g | SCENE= }}
{{STRUCTURE_2f3g| PDB=2f3g | SCENE= }}
-
'''IIAGLC CRYSTAL FORM III'''
+
===IIAGLC CRYSTAL FORM III===
-
==Overview==
+
<!--
-
In Escherichia coli, the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS), IIAGlc (IIIGlc in older literature), is also the central regulatory protein of the PTS. Depending upon its state of phosphorylation, IIAGlc binds to a number of different proteins that display no apparent sequence homology. Previous structural studies suggested that nonspecific hydrophobic interactions, specific salt bridges, and an intermolecular Zn(II) binding site contribute to the wide latitude in IIAGlc binding sites. Two new crystal forms of IIAGlc have been solved at high resolution, and the models were compared to those previously studied. The major intermolecular contacts in the crystals differ in detail, but all involve the hydrophobic active site of IIAGlc interacting with a hydrophobic patch on a neighbor and all are shown to be surprisingly similar to the physiologically relevant regulatory interaction of IIAGlc with glycerol kinase. In two crystal forms, a helix on one molecule interacts with the face of another, while in the other crystal form, the primary crystal contact consists of a strand of beta-sheet that contributes to an intermolecular Zn(II) binding site with tetrahedral ligation identical to that of the zinc peptidase thermolysin. Thus, relatively nonspecific hydrophobic interactions combined with specific salt bridges and an intermolecular cation binding site (cation-promoted association) permit a regulatory protein to bind to target proteins that have little or no sequence or structural homology with one another. It is suggested that signal transduction by IIAGlc is a binary switch in which phosphorylation at the active site directly controls binding to target molecules.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9405042}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9405042 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9405042}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:25:03 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:50:15 2008''

Revision as of 08:50, 28 July 2008

Image:2f3g.png

Template:STRUCTURE 2f3g

IIAGLC CRYSTAL FORM III

Template:ABSTRACT PUBMED 9405042

About this Structure

2F3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural studies of the Escherichia coli signal transducing protein IIAGlc: implications for target recognition., Feese MD, Comolli L, Meadow ND, Roseman S, Remington SJ, Biochemistry. 1997 Dec 23;36(51):16087-96. PMID:9405042

Page seeded by OCA on Mon Jul 28 11:50:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f3g"
Personal tools