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.


1wrs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wrs.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wrs.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wrs| PDB=1wrs | SCENE= }}
{{STRUCTURE_1wrs| PDB=1wrs | SCENE= }}
-
'''NMR STUDY OF HOLO TRP REPRESSOR'''
+
===NMR STUDY OF HOLO TRP REPRESSOR===
-
==Overview==
+
<!--
-
The solution structures of the trp-repressor from Escherichia coli in both the liganded (holo-) and unliganded (apo-) form, have been refined by restrained molecular dynamics with simulated annealing using the program XPLOR and additional experimental constraints. The ensemble of refined holorepressor structures have a root-mean-square deviation (r.m.s.d.) of 0.8 A relative to the average structure for the backbone of the dimer core (helices A, B, C, A', B', C') and 2.5 A for the helix-turn-helix DNA-binding domain (helices D and E). The corresponding values for the aporepressor are 0.9 A for the backbone of the ABC-dimer core and 3.2 A for the DE helix-turn-helix. The r.m.s.d. of the average structures from the corresponding crystal structures are 2.3 A for the holorepressor ABC core and 4.2 A for its DE region; 2.3 A for the aporepressor core and 5.5 A for its DE region. The relative disorder of the DNA-binding domain is reflected in a number of experimental parameters including substantially more rapid backbone proton exchange rates, exchange-limited relaxation times and crystallographic B-factors. The stabilizing effect of the L-Trp ligand is evident in these measurements, as it is in the higher precision of the holorepressor structure.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8433368}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8433368 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8433368}}
==About this Structure==
==About this Structure==
-
1WRS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRS OCA].
+
1WRS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRS OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Peptide]]
[[Category: Peptide]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:03:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:21:20 2008''

Revision as of 13:21, 5 July 2008

Image:1wrs.png

Template:STRUCTURE 1wrs

NMR STUDY OF HOLO TRP REPRESSOR

Template:ABSTRACT PUBMED 8433368

About this Structure

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

Reference

Refined solution structures of the Escherichia coli trp holo- and aporepressor., Zhao D, Arrowsmith CH, Jia X, Jardetzky O, J Mol Biol. 1993 Feb 5;229(3):735-46. PMID:8433368

Page seeded by OCA on Sat Jul 5 16:21:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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