1MB1

MBP1 FROM SACCHAROMYCES CEREVISIAE

Summary for 1MB1

• Entry DOI: 10.2210/pdb1mb1/pdb
• Descriptor: MLU1-BOX BINDING PROTEIN (2 entities in total)
• Functional Keywords: transcription regulation, cell-cycle, transcription factor
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P39678
• Total number of polymer chains: 1
• Total formula weight: 14900.89

Authors

Taylor, I.A.,Smerdon, S.J. (deposition date: 1997-07-23, release date: 1998-07-29, Last modification date: 2024-02-14)

Primary citation

Taylor, I.A.,Treiber, M.K.,Olivi, L.,Smerdon, S.J.
The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution.
J.Mol.Biol., 272:1-8, 1997

PubMed Abstract: The structure of the DNA-binding domain of the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 has been solved using the multiwavelength anomalous diffraction (MAD) technique on crystals of selenomethionyl protein and refined at 2.1 A resolution. The molecule is globular, consisting of a twisted, six-stranded beta-barrel that is packed against a loose bundle of four alpha-helices. Two of the beta-strands in combination with two of the helices form a structure characteristic of the DNA-binding motif found in the CAP family of helix-turn-helix transcription factors. In Mbp1, this beta2/alpha2 motif is associated with regions of both positive electrostatic potential and sequence conservation within the Mbp1/Swi4 family, suggesting a role in DNA-binding in these proteins. A combination of structural and biochemical data further indicate a similarity to HNF3gamma/fork head, a member of the family of "winged" helix-turn-helix proteins. We propose a model for DNA-binding involving a recognition helix in the major groove, phosphodiester backbone interactions through the beta-hairpin and further base and/or phosphate interactions mediated by a C-terminal, positively charged loop.

PubMed: 9299332
DOI: 10.1006/jmbi.1997.1229

Experimental method

X-RAY DIFFRACTION (2.1 Å)