1bm8

<table><tr><td colspan='2'>[[1bm8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BM8 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=1bm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm8 OCA], [https://pdbe.org/1bm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bm8 RCSB], [https://www.ebi.ac.uk/pdbsum/1bm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm8 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 ==

BACKGROUND: During the cell cycle, cells progress through four distinct phases, G1, S, G2 and M; transcriptional controls play an important role at the transition between these phases. MCB-binding factor (MBF), a transcription factor from budding yeast, binds to the so-called MCB (MluI cell-cycle box) elements found in the promoters of many DNA synthesis genes, and activates the transcription of those at the G1--&gt;S phase transition. MBF is comprised of two proteins, Mbp1 and Swi6. RESULTS: The three-dimensional structure of the N-terminal DNA-binding domain of Mbp1 has been determined by multiwavelength anomalous diffraction from crystals of the selenomethionyl variant of the protein. The structure is composed of a six-stranded beta sheet interspersed with two pairs of alpha helices. The most conserved core region among Mbp1-related transcription factors folds into a central helix-turn-helix motif with a short N-terminal beta strand and a C-terminal beta hairpin. CONCLUSIONS: Despite little sequence similarity, the structure within the core region of the Mbp1 N-terminal domain exhibits a similar fold to that of the DNA-binding domains of other proteins, such as hepatocyte nuclear factor-3gamma and histone H5 from eukaryotes, and the prokaryotic catabolite gene activator. However, the structure outside the core region defines Mbp1 as a larger entity with substructures that stabilize and display the helix-turn-helix motif.

Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis.,Xu RM, Koch C, Liu Y, Horton JR, Knapp D, Nasmyth K, Cheng X Structure. 1997 Mar 15;5(3):349-58. PMID:9083114<ref>PMID:9083114</ref>

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

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== References ==

<references/>

[[Category: Cheng, X]]

[[Category: Horton, J R]]

[[Category: Knapp, D]]

[[Category: Koch, C]]

[[Category: Liu, Y]]

[[Category: Nasmyth, K]]

[[Category: Xu, R M]]

[[Category: Transcription factor]]