1TRO
CRYSTAL STRUCTURE OF TRP REPRESSOR OPERATOR COMPLEX AT ATOMIC RESOLUTION
Summary for 1TRO
| Entry DOI | 10.2210/pdb1tro/pdb |
| Descriptor | DNA (5'-D(*TP*GP*TP*AP*CP*TP*AP*GP*TP*TP*AP*AP*CP*TP*AP*GP*T P*AP*C)-3'), PROTEIN (TRP REPRESSOR), TRYPTOPHAN, ... (4 entities in total) |
| Functional Keywords | protein-dna complex, double helix, transcription-dna complex, transcription/dna |
| Biological source | Escherichia coli str. K12 substr. |
| Total number of polymer chains | 8 |
| Total formula weight | 73576.54 |
| Authors | Otwinowski, Z.,Schevitz, R.W.,Zhang, R.-G.,Lawson, C.L.,Joachimiak, A.,Marmorstein, R.,Luisi, B.F.,Sigler, P.B. (deposition date: 1992-08-30, release date: 1994-01-31, Last modification date: 2024-02-14) |
| Primary citation | Otwinowski, Z.,Schevitz, R.W.,Zhang, R.G.,Lawson, C.L.,Joachimiak, A.,Marmorstein, R.Q.,Luisi, B.F.,Sigler, P.B. Crystal structure of trp repressor/operator complex at atomic resolution. Nature, 335:321-329, 1988 Cited by PubMed Abstract: 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. PubMed: 3419502DOI: 10.1038/335321a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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