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.

1sw5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sw5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sw5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sw5| PDB=1sw5 | SCENE= }}
{{STRUCTURE_1sw5| PDB=1sw5 | SCENE= }}
-
'''Crystal structure of ProX from Archeoglobus fulgidus in the ligand free form'''
+
===Crystal structure of ProX from Archeoglobus fulgidus in the ligand free form===
-
==Overview==
+
<!--
-
Compatible solutes such as glycine betaine and proline betaine serve as protein stabilizers because of their preferential exclusion from protein surfaces. To use extracellular sources of this class of compounds as osmo-, cryo-, or thermoprotectants, Bacteria and Archaea have developed high affinity uptake systems of the ATP-binding cassette type. These transport systems require periplasmic- or extracellular-binding proteins that are able to bind the transported substance with high affinity. Therefore, binding proteins that bind compatible solutes have to avoid the exclusion of their ligands within the binding pocket. In the present study we addressed the question to how compatible solutes can be effectively bound by a protein at temperatures around 83 degrees C as this is done by the ligand-binding protein ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus. We solved the structures of ProX without ligand and in complex with both of its natural ligands glycine betaine and proline betaine, as well as in complex with the artificial ligand trimethylammonium. Cation-pi interactions and non-classical hydrogen bonds between four tyrosine residues, a main chain carbonyl oxygen, and the ligand have been identified to be the key determinants in binding the quaternary amines of the three investigated ligands. The comparison of the ligand binding sites of ProX from A. fulgidus and the recently solved structure of ProX from Escherichia coli revealed a very similar solution for the problem of compatible solute binding, although both proteins share only a low degree of sequence identity. The residues involved in ligand binding are functionally equivalent but not conserved in the primary sequence.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15308642}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15308642 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15308642}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Compatible solute]]
[[Category: Compatible solute]]
[[Category: Non-classical hydrogen bond]]
[[Category: Non-classical hydrogen bond]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:12:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:41:49 2008''

Revision as of 10:41, 29 July 2008

Image:1sw5.png

Template:STRUCTURE 1sw5

Crystal structure of ProX from Archeoglobus fulgidus in the ligand free form

Template:ABSTRACT PUBMED 15308642

About this Structure

1SW5 is a Single protein structure of sequence from Archaeoglobus fulgidus dsm 4304. Full crystallographic information is available from OCA.

Reference

Structural basis for the binding of compatible solutes by ProX from the hyperthermophilic archaeon Archaeoglobus fulgidus., Schiefner A, Holtmann G, Diederichs K, Welte W, Bremer E, J Biol Chem. 2004 Nov 12;279(46):48270-81. Epub 2004 Aug 11. PMID:15308642

Page seeded by OCA on Tue Jul 29 13:41:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sw5"
Personal tools