We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2gbp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gbp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2gbp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gbp| PDB=2gbp | SCENE= }}
{{STRUCTURE_2gbp| PDB=2gbp | SCENE= }}
-
'''SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI GALACTOSE CHEMORECEPTOR PROTEIN'''
+
===SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI GALACTOSE CHEMORECEPTOR PROTEIN===
-
==Overview==
+
<!--
-
D-galactose-binding (or chemoreceptor) protein of Escherichia coli serves as an initial component for both chemotaxis towards galactose and glucose and high-affinity active transport of the two sugars. Well-refined x-ray structures of the liganded forms of the wild-type and a mutant protein isolated from a strain defective in chemotaxis but fully competent in transport have provided a molecular view of the sugar-binding site and of a site for interacting with the Trg transmembrane signal transducer. The geometry of the sugar-binding site, located in the cleft between the two lobes of the bilobate protein, is novel in that it is designed for tight binding and sequestering of either the alpha or beta anomer of the D-stereoisomer of the 4-epimers galactose and glucose. Binding specificity and affinity are conferred primarily by polar planar side-chain residues that form intricate networks of cooperative and bidentate hydrogen bonds with the sugar substrates, and secondarily by aromatic residues that sandwich the pyranose ring. Each of the pairs of anomeric hydroxyls and epimeric hydroxyls is recognized by a distinct Asp residue. The site for interaction with the transducer is about 18 A from the sugar-binding site. Mutation of Gly74 to Asp at this site, concomitant with considerable changes in the local ordered water structures, contributes to the lack of productive interaction with the transmembrane signal transducer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_3057628}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 3057628 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_3057628}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Vyas, N K.]]
[[Category: Vyas, N K.]]
[[Category: Periplasmic binding protein]]
[[Category: Periplasmic binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:55:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:18:50 2008''

Revision as of 06:18, 28 July 2008

Image:2gbp.png

Template:STRUCTURE 2gbp

SUGAR AND SIGNAL-TRANSDUCER BINDING SITES OF THE ESCHERICHIA COLI GALACTOSE CHEMORECEPTOR PROTEIN

Template:ABSTRACT PUBMED 3057628

About this Structure

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

Reference

Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein., Vyas NK, Vyas MN, Quiocho FA, Science. 1988 Dec 2;242(4883):1290-5. PMID:3057628

Page seeded by OCA on Mon Jul 28 09:18:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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