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.


2q88

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2q88.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2q88.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2q88| PDB=2q88 | SCENE= }}
{{STRUCTURE_2q88| PDB=2q88 | SCENE= }}
-
'''Crystal structure of EhuB in complex with ectoine'''
+
===Crystal structure of EhuB in complex with ectoine===
-
==Overview==
+
<!--
-
In microorganisms, members of the binding-protein-dependent ATP-binding cassette transporter superfamily constitute an important class of transport systems. Some of them are involved in osmoprotection under hyperosmotic stress by facilitating the uptake of "compatible solutes". Currently, the molecular mechanisms used by these transport systems to recognize compatible solutes are limited to transporters specific for glycine betaine and proline betaine. Therefore, this study reports a detailed analysis of the molecular principles governing substrate recognition in the Ehu system from Sinorhizobium meliloti, which is responsible for the uptake of the compatible solutes ectoine and hydroxyectoine. To contribute to a broader understanding of the molecular interactions underlying substrate specificity, our study focused on the substrate-binding protein EhuB because this protein binds the ligand selectively, delivers it to the translocation machinery in the membrane and is thought to be responsible for substrate specificity. The crystal structures of EhuB, in complex with ectoine and hydroxyectoine, were determined at a resolution of 1.9 A and 2.3 A, respectively, and allowed us to assign the structural principles of substrate recognition and binding. Based on these results, site-directed mutagenesis of amino acids involved in ligand binding was employed to address their individual contribution to complex stability. A comparison with the crystal structures of other binding proteins specific for compatible solutes revealed common principles of substrate recognition, but also important differences that might be an adaptation to the nature of the ligand and to the demands on protein affinity imposed by the environment.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17996893}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17996893 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17996893}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Substrate-binding protein]]
[[Category: Substrate-binding protein]]
[[Category: Transport protein]]
[[Category: Transport protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:31:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:05:55 2008''

Revision as of 00:05, 29 July 2008

Image:2q88.png

Template:STRUCTURE 2q88

Crystal structure of EhuB in complex with ectoine

Template:ABSTRACT PUBMED 17996893

About this Structure

2Q88 is a Single protein structure of sequence from Sinorhizobium meliloti. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand-binding protein EhuB from Sinorhizobium meliloti reveals substrate recognition of the compatible solutes ectoine and hydroxyectoine., Hanekop N, Hoing M, Sohn-Bosser L, Jebbar M, Schmitt L, Bremer E, J Mol Biol. 2007 Dec 14;374(5):1237-50. Epub 2007 Sep 29. PMID:17996893

Page seeded by OCA on Tue Jul 29 03:05:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q88"
Personal tools