1bm8
From Proteopedia
(New page: 200px<br /><applet load="1bm8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bm8, resolution 1.71Å" /> '''DNA-BINDING DOMAIN O...) |
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| - | [[Image:1bm8.jpg|left|200px]]<br /><applet load="1bm8" size=" | + | [[Image:1bm8.jpg|left|200px]]<br /><applet load="1bm8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bm8, resolution 1.71Å" /> | caption="1bm8, resolution 1.71Å" /> | ||
'''DNA-BINDING DOMAIN OF MBP1'''<br /> | '''DNA-BINDING DOMAIN OF MBP1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: During the cell cycle, cells progress through four distinct | + | 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== | ==About this Structure== | ||
| - | 1BM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1BM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
| - | [[Category: Horton, J | + | [[Category: Horton, J R.]] |
[[Category: Knapp, D.]] | [[Category: Knapp, D.]] | ||
[[Category: Koch, C.]] | [[Category: Koch, C.]] | ||
[[Category: Liu, Y.]] | [[Category: Liu, Y.]] | ||
[[Category: Nasmyth, K.]] | [[Category: Nasmyth, K.]] | ||
| - | [[Category: Xu, R | + | [[Category: Xu, R M.]] |
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
[[Category: cyclins]] | [[Category: cyclins]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:48 2008'' |
Revision as of 09:56, 21 February 2008
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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
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