1wrs: Difference between revisions
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[[Image:1wrs.gif|left|200px]] | [[Image:1wrs.gif|left|200px]] | ||
'''NMR STUDY OF HOLO TRP REPRESSOR''' | {{Structure | ||
|PDB= 1wrs |SIZE=350|CAPTION= <scene name='initialview01'>1wrs</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NMR STUDY OF HOLO TRP REPRESSOR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WRS is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8433368 8433368] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:00:44 2008'' | ||
Revision as of 13:00, 20 March 2008
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| Ligands: | TRP | ||||||||||||
| 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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