1lih

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lih.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lih.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lih| PDB=1lih | SCENE= }}
{{STRUCTURE_1lih| PDB=1lih | SCENE= }}
-
'''THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND'''
+
===THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND===
-
==Overview==
+
<!--
-
The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1660187}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1660187 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1660187}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Yeh, J I.]]
[[Category: Yeh, J I.]]
[[Category: Chemotaxis]]
[[Category: Chemotaxis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:57:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:58:37 2008''

Revision as of 17:58, 2 July 2008

Image:1lih.png

Template:STRUCTURE 1lih

THREE-DIMENSIONAL STRUCTURES OF THE LIGAND-BINDING DOMAIN OF THE BACTERIAL ASPARTATE RECEPTOR WITH AND WITHOUT A LIGAND

Template:ABSTRACT PUBMED 1660187

About this Structure

1LIH is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand., Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, Jancarik J, Koshland DE Jr, Kim SH, Science. 1991 Nov 29;254(5036):1342-7. PMID:1660187

Page seeded by OCA on Wed Jul 2 20:58:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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