1wrs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1wrs.gif|left|200px]]
[[Image:1wrs.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1wrs |SIZE=350|CAPTION= <scene name='initialview01'>1wrs</scene>
+
The line below this paragraph, containing "STRUCTURE_1wrs", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1wrs| PDB=1wrs | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrs OCA], [http://www.ebi.ac.uk/pdbsum/1wrs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wrs RCSB]</span>
+
-
}}
+
'''NMR STUDY OF HOLO TRP REPRESSOR'''
'''NMR STUDY OF HOLO TRP REPRESSOR'''
Line 27: Line 24:
[[Category: Zhao, D.]]
[[Category: Zhao, D.]]
[[Category: Zheng, Z.]]
[[Category: Zheng, Z.]]
-
[[Category: dna-binding]]
+
[[Category: Dna-binding]]
-
[[Category: operon repressor]]
+
[[Category: Operon repressor]]
-
[[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 Mon Mar 31 00:40:10 2008''
+

Revision as of 11:03, 3 May 2008

Template:STRUCTURE 1wrs

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.

About this Structure

1WRS is a Single protein structure of sequence from Escherichia coli. Full crystallographic 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 May 3 14:03:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools