1tro: Difference between revisions
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|PDB= 1tro |SIZE=350|CAPTION= <scene name='initialview01'>1tro</scene>, resolution 1.900Å | |PDB= 1tro |SIZE=350|CAPTION= <scene name='initialview01'>1tro</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tro OCA], [http://www.ebi.ac.uk/pdbsum/1tro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tro RCSB]</span> | |||
}} | }} | ||
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[[Category: Sigler, P B.]] | [[Category: Sigler, P B.]] | ||
[[Category: Zhang, R G.]] | [[Category: Zhang, R G.]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:00:10 2008'' | ||
Revision as of 21:00, 30 March 2008
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| 1tro, resolution 1.900Å | |||||||||||||
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| Ligands: | DA, DC, DG, DT, TRP | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION
Overview
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.
About this Structure
1TRO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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