|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==NMR STUDY OF APO TRP REPRESSOR== | | ==NMR STUDY OF APO TRP REPRESSOR== |
| - | <StructureSection load='1wrt' size='340' side='right'caption='[[1wrt]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1wrt' size='340' side='right'caption='[[1wrt]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wrt]] is a 2 chain structure with 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=1WRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WRT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wrt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WRT FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrt OCA], [http://pdbe.org/1wrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wrt RCSB], [http://www.ebi.ac.uk/pdbsum/1wrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrt ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrt OCA], [https://pdbe.org/1wrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wrt RCSB], [https://www.ebi.ac.uk/pdbsum/1wrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI]] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. | + | [https://www.uniprot.org/uniprot/TRPR_ECOLI TRPR_ECOLI] This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 34: |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Zhao, D]] | + | [[Category: Zhao D]] |
| - | [[Category: Zheng, Z]] | + | [[Category: Zheng Z]] |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Operon repressor]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| Structural highlights
Function
TRPR_ECOLI This protein is an aporepressor. When complexed with L-tryptophan it binds the operator region of the trp operon (5'-ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao D, Arrowsmith CH, Jia X, Jardetzky O. Refined solution structures of the Escherichia coli trp holo- and aporepressor. J Mol Biol. 1993 Feb 5;229(3):735-46. PMID:8433368 doi:http://dx.doi.org/10.1006/jmbi.1993.1076
|
