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.


1xxc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xxc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1xxc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xxc| PDB=1xxc | SCENE= }}
{{STRUCTURE_1xxc| PDB=1xxc | SCENE= }}
-
'''C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR'''
+
===C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR===
-
==Overview==
+
<!--
-
The structure of the oligomerization and L-arginine binding domain of the Escherichia coli arginine repressor (ArgR) has been determined using X-ray diffraction methods at 2.2 A resolution with bound arginine and at 2.8 A in the unliganded form. The oligomeric core is a 3-fold rotationally symmetric hexamer formed from six identical subunits corresponding to the 77 C-terminal residues (80 to 156) of ArgR. Each subunit has an alpha/beta fold containing a four-stranded antiparallel beta-sheet and two antiparallel alpha-helices. The hexamer is formed from two trimers, each with tightly packed hydrophobic cores. In the absence of arginine, the trimers stack back-to-back through a dyad-symmetric, sparsely packed hydrophobic interface. Six molecules of arginine bind at the trimer-trimer interface, each making ten hydrogen bonds to the protein including a direct ion pair that crosslinks the two protein trimers. Solution experiments with wild-type ArgR and oligomerization domain indicate that the hexameric form is greatly stabilized upon arginine binding. The crystal structures and solution experiments together suggest possible mechanisms of how arginine activates ArgR to bind to its DNA targets and provides a stereochemical basis for interpreting the results of mutagenesis and biochemical experiments with ArgR.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8594204}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8594204 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8594204}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Sigler, P B.]]
[[Category: Sigler, P B.]]
[[Category: Dna binding regulatory protein]]
[[Category: Dna binding regulatory protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:37:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:32:09 2008''

Revision as of 02:32, 28 July 2008

Image:1xxc.png

Template:STRUCTURE 1xxc

C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR

Template:ABSTRACT PUBMED 8594204

About this Structure

1XXC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli., Van Duyne GD, Ghosh G, Maas WK, Sigler PB, J Mol Biol. 1996 Feb 23;256(2):377-91. PMID:8594204

Page seeded by OCA on Mon Jul 28 05:32:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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