Motion in S. cerevisiae PPR1 Zn-finger DNA recognition protein. [ppr1]

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Classification Known Subunit Motion, Not Involving Allostery [S-n-2]

Structures 1PYI PPR1-DNA complex, S. cerevisiae [ PartsList ]

Description GAL-anaologous Zn-finger DNA binding protein. Structure solved complex to 14-bp consensus DNA sequence in 1994. Upon binding DNA, PPR1 dimerizes into asymmetric coiled coiled homodimer. Protein motion may be simulated by superimposing one bound asymmetric homodimer onto another, as in Figure 6 of Marmorstein et al. Alternatively, may be compared with unbound monomer (structure?) or GAL4, with which it is homologous.

Particular values describing motion Creation Date = 19970822 Modification Date = 19970822 Experimental Methods = x (Traditional x-ray)

References R Marmorstein and S C Harrison (1994). Crystal structure of a PPR1-DNA complex: DNA recognition by proteins containing a Zn2Cys6 binuclear cluster. Gen. & Devlop. 8:2504-2412. [Medline info for 94278498]

GO terms associated with structures Molecular function DNA binding, zinc ion binding, transcription factor activity Cellular component nucleus Biological process transcription, regulation of transcription, DNA-dependent

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