1wrs
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |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> | ||
}} | }} | ||
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[[Category: Zhao, D.]] | [[Category: Zhao, D.]] | ||
[[Category: Zheng, Z.]] | [[Category: Zheng, Z.]] | ||
| - | [[Category: TRP]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: operon repressor]] | [[Category: operon repressor]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:40:10 2008'' |
Revision as of 21:40, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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