1bm8
From Proteopedia
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'''DNA-BINDING DOMAIN OF MBP1''' | '''DNA-BINDING DOMAIN OF MBP1''' | ||
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[[Category: Nasmyth, K.]] | [[Category: Nasmyth, K.]] | ||
[[Category: Xu, R M.]] | [[Category: Xu, R M.]] | ||
| - | [[Category: | + | [[Category: Cell cycle]] |
| - | [[Category: | + | [[Category: Cyclin]] |
| - | [[Category: | + | [[Category: Dna synthesis]] |
| - | [[Category: | + | [[Category: Helix-turn-helix dna-binding domain]] |
| - | [[Category: | + | [[Category: Multiwavelength anomalous diffraction]] |
| - | [[Category: | + | [[Category: Transcription factor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:41, 2 May 2008
DNA-BINDING DOMAIN OF MBP1
Overview
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-->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.
About this Structure
1BM8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 11:41:33 2008
