1tro
From Proteopedia
(Difference between revisions)
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<StructureSection load='1tro' size='340' side='right'caption='[[1tro]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1tro' size='340' side='right'caption='[[1tro]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1tro]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1tro]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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'>[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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1tro ConSurf]. | </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=1tro ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:3419502</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1tro" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli str. K-12 substr. W3110]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Joachimiak | + | [[Category: Joachimiak A]] |
| - | [[Category: Lawson | + | [[Category: Lawson CL]] |
| - | [[Category: Luisi | + | [[Category: Luisi BF]] |
| - | [[Category: Marmorstein | + | [[Category: Marmorstein R]] |
| - | [[Category: Otwinowski | + | [[Category: Otwinowski Z]] |
| - | [[Category: Schevitz | + | [[Category: Schevitz RW]] |
| - | [[Category: Sigler | + | [[Category: Sigler PB]] |
| - | [[Category: Zhang | + | [[Category: Zhang R-G]] |
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Current revision
CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION
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