1mb1

<table><tr><td colspan='2'>[[1mb1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MB1 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mb1 OCA], [https://pdbe.org/1mb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mb1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mb1 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/MBP1_YEAST MBP1_YEAST]] Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle.

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== Publication Abstract from PubMed ==

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.

The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1 A resolution.,Taylor IA, Treiber MK, Olivi L, Smerdon SJ J Mol Biol. 1997 Sep 12;272(1):1-8. PMID:9299332<ref>PMID:9299332</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Smerdon, S J]]

[[Category: Taylor, I A]]

[[Category: Cell-cycle]]

[[Category: Transcription regulation]]