1wrt: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1wrt.png|left|200px]]


<!--
==NMR STUDY OF APO TRP REPRESSOR==
The line below this paragraph, containing "STRUCTURE_1wrt", creates the "Structure Box" on the page.
<StructureSection load='1wrt' size='340' side='right'caption='[[1wrt]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1wrt|  PDB=1wrt  |  SCENE=  }}
</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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wr/1wrt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wrt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===NMR STUDY OF APO TRP REPRESSOR===
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<ref>PMID:8433368</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_8433368}}, adds the Publication Abstract to the page
<div class="pdbe-citations 1wrt" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 8433368 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_8433368}}
__TOC__
 
</StructureSection>
==About this Structure==
1WRT is a 2 chains structure of sequences 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].
 
==Reference==
<ref group="xtra">PMID:8433368</ref><references group="xtra"/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Zhao, D.]]
[[Category: Large Structures]]
[[Category: Zheng, Z.]]
[[Category: Zhao D]]
[[Category: Dna-binding]]
[[Category: Zheng Z]]
[[Category: Operon repressor]]
[[Category: Transcription regulation]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:37:18 2009''
Retrieved from "https://proteopedia.org/1wrt"