2orc | pdb_00002orc

CRO REPRESSOR INSERTION MUTANT K56-[DGEVK], NMR, 32 STRUCTURES

spinqualitylabelsall models 2orc, 32 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2orc is a 1 chain structure with sequence from Bacteriophage lambda. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: CRO MUTANT K56-[DGEVK] (Bacteriophage lambda) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RCRO_LAMBD] Cro represses genes normally expressed in early phage development and is necessary for the late stage of lytic growth. It does this by binding to the OL and OR operators regions normally used by the repressor protein for lysogenic maintenance. 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 solution structure of a monomeric variant of the lambda Cro repressor has been determined by multidimensional NMR. Cro K56[DGEVK] differs from wild-type Cro by the insertion of five amino acids at the center of the dimer interface. 1H and 15N resonances for 70 of the 71 residues have been assigned. Thirty-two structures were calculated by hybrid distance geometry/simulated annealing methods using 463 NOE-distance restraints, 26 hydrogen-bond, and 39 dihedral-angle restraints. The root-mean-square deviation (RMSD) from the average structure for atoms in residues 3-60 is 1.03 +/- 0.44 A for the peptide backbone and 1.6 +/- 0.73 A for all nonhydrogen atoms. The overall structure conforms very well to the original design. Although the five inserted residues form a beta hairpin as expected, this engineered turn as well as other turns in the structure are not well defined by the NMR data. Dynamics studies of backbone amides reveal T1/T2 ratios of residues in the alpha2-alpha3, beta2-beta3, and engineered turn that are reflective of chemical exchange or internal motion. The solution structure and dynamics are discussed in light of the conformational variation that has been observed in other Cro structures, and the importance of flexibility in DNA recognition. Solution structure and dynamics of a designed monomeric variant of the lambda Cro repressor.,Mossing MC Protein Sci. 1998 Apr;7(4):983-93. PMID:9568905 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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