1tns
From Proteopedia
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| - | [[Image:1tns.gif|left|200px]] | + | [[Image:1tns.gif|left|200px]] |
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| - | '''A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE''' | + | {{Structure |
| + | |PDB= 1tns |SIZE=350|CAPTION= <scene name='initialview01'>1tns</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TNS is a [ | + | 1TNS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TNS OCA]. |
==Reference== | ==Reference== | ||
| - | A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase., Clubb RT, Omichinski JG, Savilahti H, Mizuuchi K, Gronenborn AM, Clore GM, Structure. 1994 Nov 15;2(11):1041-8. PMID:[http:// | + | A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase., Clubb RT, Omichinski JG, Savilahti H, Mizuuchi K, Gronenborn AM, Clore GM, Structure. 1994 Nov 15;2(11):1041-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7881904 7881904] |
[[Category: Enterobacteria phage mu]] | [[Category: Enterobacteria phage mu]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:53 2008'' |
Revision as of 12:20, 20 March 2008
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A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING DOMAIN OF MU TRANSPOSASE
Overview
BACKGROUND: Mu transposase (MuA) is a multidomain protein encoded by the bacteriophage Mu genome. It is responsible for translocation of the Mu genome, which is the largest and most efficient transposon known. While the various domains of MuA have been delineated by means of biochemical methods, no data have been obtained to date relating to its tertiary structure. RESULTS: We have solved the three-dimensional solution structure of the DNA-binding domain (residues 1-76; MuA76) of MuA by multidimensional heteronuclear NMR spectroscopy. The structure consists of a three-membered alpha-helical bundle buttressed by a three-stranded antiparallel beta-sheet. Helices H1 and H2 and the seven-residue turn connecting them comprise a helix-turn-helix (HTH) motif. In addition, there is a long nine-residue flexible loop or wing connecting strands B2 and B3 of the sheet. NMR studies of MuA76 complexed with a consensus DNA site from the internal activation region of the Mu genome indicate that the wing and the second helix of the HTH motif are significantly perturbed upon DNA binding. CONCLUSIONS: While the general appearance of the DNA-binding domain of MuA76 is similar to that of other winged HTH proteins, the connectivity of the secondary structure elements is permuted. Hence, the fold of MuA76 represents a novel class of winged HTH DNA-binding domain.
About this Structure
1TNS is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase., Clubb RT, Omichinski JG, Savilahti H, Mizuuchi K, Gronenborn AM, Clore GM, Structure. 1994 Nov 15;2(11):1041-8. PMID:7881904
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