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1tro

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Revision as of 11:27, 16 February 2022

CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION

Structural highlights

1tro is a 8 chain structure with sequence from Ecow3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 crystal structure of the trp repressor/operator complex shows an extensive contact surface, including 24 direct and 6 solvent-mediated hydrogen bonds to the phosphate groups of the DNA. There are no direct hydrogen bonds or non-polar contacts to the bases that can explain the repressor's specificity for the operator sequence. Rather, the sequence seems to be recognized indirectly through its effects on the geometry of the phosphate backbone, which in turn permits the formation of a stable interface. Water-mediated polar contacts to the bases also appear to contribute part of the specificity.

Crystal structure of trp repressor/operator complex at atomic resolution.,Otwinowski Z, Schevitz RW, Zhang RG, Lawson CL, Joachimiak A, Marmorstein RQ, Luisi BF, Sigler PB Nature. 1988 Sep 22;335(6188):321-9. PMID:3419502^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Otwinowski Z, Schevitz RW, Zhang RG, Lawson CL, Joachimiak A, Marmorstein RQ, Luisi BF, Sigler PB. Crystal structure of trp repressor/operator complex at atomic resolution. Nature. 1988 Sep 22;335(6188):321-9. PMID:3419502 doi:http://dx.doi.org/10.1038/335321a0

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tro"

@@ Line 3: / Line 3: @@
 <StructureSection load='1tro' size='340' side='right'caption='[[1tro]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tro]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TRO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tro]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TRO FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tro OCA], [http://pdbe.org/1tro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tro RCSB], [http://www.ebi.ac.uk/pdbsum/1tro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tro ProSAT]</span></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=1tro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tro OCA], [https://pdbe.org/1tro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tro RCSB], [https://www.ebi.ac.uk/pdbsum/1tro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tro ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1tro

From Proteopedia

Revision as of 11:27, 16 February 2022

CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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