1mi7

Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) IsopropanolCrystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol

Structural highlights 1mi7 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1wrp, 2wrp, 3wrp, 1tro, 1trr Gene: trpR (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum 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 E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol. E. coli trp repressor forms a domain-swapped array in aqueous alcohol.,Lawson CL, Benoff B, Berger T, Berman HM, Carey J Structure. 2004 Jun;12(6):1099-108. PMID:15274929 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1mi7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image