View source for 5tm0


==Solution NMR structures of two alternative conformations of E. coli tryptophan repressor in dynamic equilibrium==
<StructureSection load='5tm0' size='340' side='right'caption='[[5tm0]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tm0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TM0 FirstGlance]. <br>
</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=5tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tm0 OCA], [https://pdbe.org/5tm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tm0 RCSB], [https://www.ebi.ac.uk/pdbsum/5tm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tm0 ProSAT]</span></td></tr>
</table>
== Function ==
[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.
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== Publication Abstract from PubMed ==
The nature of flexibility in the helix-turn-helix region of E. coli trp aporepressor has been unexplained for many years. The original ensemble of nuclear magnetic resonance (NMR structures showed apparent disorder, but chemical shift and relaxation measurements indicated a helical region. Nuclear Overhauser effect (NOE) data for a temperature-sensitive mutant showed more helical character in its helix-turn-helix region, but nevertheless also led to an apparently disordered ensemble. However, conventional NMR structure determination methods require all structures in the ensemble to be consistent with every NOE simultaneously. This work uses an alternative approach in which some structures of the ensemble are allowed to violate some NOEs to permit modeling of multiple conformational states that are in dynamic equilibrium. Newly measured NOE data for wild-type aporepressor are used as time-averaged distance restraints in molecular dynamics simulations to generate an ensemble of helical conformations that is more consistent with the observed NMR data than the apparent disorder in the previously reported NMR structures. The results indicate the presence of alternating helical conformations that provide a better explanation for the flexibility of the helix-turn-helix region of trp aporepressor. Structures representing these conformations have been deposited with PDB ID: 5TM0. Proteins 2017; 85:731-740. (c) 2016 Wiley Periodicals, Inc.

Multiple helical conformations of the helix-turn-helix region revealed by NOE-restrained MD simulations of tryptophan aporepressor, TrpR.,Harish B, Swapna GV, Kornhaber GJ, Montelione GT, Carey J Proteins. 2017 Apr;85(4):731-740. doi: 10.1002/prot.25252. Epub 2017 Feb 22. PMID:28120439<ref>PMID:28120439</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5tm0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Carey J]]
[[Category: Harish B]]
[[Category: Kornhaber GJ]]
[[Category: Montelione GT]]
[[Category: Swapna GVT]]