A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex
The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal struc...
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| Veröffentlicht in: | Nature (London) 1996-04, Vol.380 (6573), p.456-460 |
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| creator | KODANDAPANI, R PIO, F NI, C.-Z PICCIALLI, G KLEMSZ, M MCKERCHER, S MAKI, R. A ELY, K. R |
| description | The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand. |
| doi_str_mv | 10.1038/380456a0 |
| format | Article |
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A ; ELY, K. R</creator><creatorcontrib>KODANDAPANI, R ; PIO, F ; NI, C.-Z ; PICCIALLI, G ; KLEMSZ, M ; MCKERCHER, S ; MAKI, R. A ; ELY, K. R</creatorcontrib><description>The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/380456a0</identifier><identifier>PMID: 8602247</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Amino Acid Sequence ; Amino acids ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; Crystallography, X-Ray ; Deoxyribonucleic acid ; DNA ; DNA - chemistry ; DNA - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Fundamental and applied biological sciences. 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R</creatorcontrib><title>A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex</title><title>Nature (London)</title><addtitle>Nature</addtitle><description>The Ets family of transcription factors, of which there are now about 35 members regulate gene expression during growth and development. They share a conserved domain of around 85 amino acids which binds as a monomer to the DNA sequence 5'-C/AGGAA/T-3'. We have determined the crystal structure of an ETS domain complexed with DNA, at 2.3-A resolution. The domain is similar to alpha + beta (winged) 'helix-turn-helix' proteins and interacts with a ten-base-pair region of duplex DNA which takes up a uniform curve of 8 degrees. The domain contacts the DNA by a novel loop-helix-loop architecture. Four of amino acids that directly interact with the DNA are highly conserved: two arginines from the recognition helix lying in the major groove, one lysine from the 'wing' that binds upstream of the core GGAA sequence, and another lysine, from the 'turn' of the 'helix-turn-helix' motif, which binds downstream and on the opposite strand.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Crystallography, X-Ray</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes</subject><subject>Helix-Turn-Helix Motifs</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Retroviridae Proteins, Oncogenic</subject><subject>Sequence Homology, Amino Acid</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0ktLAzEQB_AgitYq-AWEIOItOnlOciz1CaKCevGypLtZ3bIvd7dav71BiwcvPc3A_JjDf4aQAw6nHKQ9kxaUNh42yIgrNEwZi5tkBCAsAyvNDtnt-zkAaI5qm2xbA0IoHJGXCa3DJ239MISupnnT0bdQFks2LLqa_bS0C2nzWhdD0dSx_wi-DBmdfdHhLdCH51NOL54eWdZUvqjZ-d2Epk3VlmG5R7ZyX_Zhf1XH5Pny4ml6zW7vr26mk1vWSq0HZhWANwaFl06o3AkRZI6CK-cgFpQGMfXa6FzZNHNahMyhRD4zHLlMczkmJ7972655X4R-SKqiT0NZ-jo0iz5BdEYbVGuhNDE7DbAWCs6tcnI95AhKAboIj_7BeRMDjrEkIhIUSpmIDldoMatClrRdUfnuK1kdK86PV3Pfp77MO1-nRf_HZHwBabT8Br5GnNo</recordid><startdate>19960404</startdate><enddate>19960404</enddate><creator>KODANDAPANI, R</creator><creator>PIO, F</creator><creator>NI, C.-Z</creator><creator>PICCIALLI, G</creator><creator>KLEMSZ, M</creator><creator>MCKERCHER, S</creator><creator>MAKI, R. 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| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1996-04, Vol.380 (6573), p.456-460 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino acids Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences Crystallography, X-Ray Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Fundamental and applied biological sciences. Psychology Genes Helix-Turn-Helix Motifs Humans Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Binding Protein Conformation Proteins Retroviridae Proteins, Oncogenic Sequence Homology, Amino Acid |
| title | A new pattern for helix-turn-helix recognition revealed by the PU.1 ETS-domain-DNA complex |
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