Motion in E. coli. Periplasmic Dipeptide Binding Protein [ecpdpbp]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures 1DPE Conformation 2 [ PartsList ] 1DPP Conformation 1 [ PartsList ]

Description An example of hinge motion between domains, the E. coli periplasmic dipeptide binding protein is larger than other periplasmic binding proteins, although similar in structure and motion. This protein has a phosphate-binding protein fold.

Particular values describing motion Creation Date = 19971130 Experimental Methods = x (Traditional x-ray) Modification Date = 1999-06-09 14:08:26.000

References Biochemistry 1995 Dec 26;34(51):16585-95 2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor. Nickitenko AV, Trakhanov S, Quiocho FA [Medline info for 96118375] Dunten PW, Harris JH, Feiz V, Mowbray SL (1993). Crystallization and preliminary X-ray analysis of the periplasmic dipeptide binding protein from Escherichia coli. Mol Biol 231(1):145-147. [Medline info for 93267646] Olson ER, Dunyak DS, Jurss LM, Poorman RA (1991). Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein. J Bacteriol 173(1):234-244. [Medline info for 91100289] Verkamp E, Backman VM, Bjornsson JM, Soll D, Eggertsson G (1993). The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. J Bacteriol 175(5):1452-1456. [Medline info for 93186713]

GO terms associated with structures Molecular function transporter activity Biological process transport

Morphs

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Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu