1qey
From Proteopedia
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| - | [[Image:1qey.gif|left|200px]] | + | [[Image:1qey.gif|left|200px]] |
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| - | '''NMR STRUCTURE DETERMINATION OF THE TETRAMERIZATION DOMAIN OF THE MNT REPRESSOR: AN ASYMMETRIC A-HELICAL ASSEMBLY IN SLOW EXCHANGE''' | + | {{Structure |
| + | |PDB= 1qey |SIZE=350|CAPTION= <scene name='initialview01'>1qey</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR STRUCTURE DETERMINATION OF THE TETRAMERIZATION DOMAIN OF THE MNT REPRESSOR: AN ASYMMETRIC A-HELICAL ASSEMBLY IN SLOW EXCHANGE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QEY is a [ | + | 1QEY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QEY OCA]. |
==Reference== | ==Reference== | ||
| - | The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils., Nooren IM, Kaptein R, Sauer RT, Boelens R, Nat Struct Biol. 1999 Aug;6(8):755-9. PMID:[http:// | + | The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils., Nooren IM, Kaptein R, Sauer RT, Boelens R, Nat Struct Biol. 1999 Aug;6(8):755-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10426954 10426954] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
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[[Category: transcriptional control]] | [[Category: transcriptional control]] | ||
| - | ''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 13:36:27 2008'' |
Revision as of 11:36, 20 March 2008
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NMR STRUCTURE DETERMINATION OF THE TETRAMERIZATION DOMAIN OF THE MNT REPRESSOR: AN ASYMMETRIC A-HELICAL ASSEMBLY IN SLOW EXCHANGE
Overview
The tetrameric Mnt repressor is involved in the genetic switch between the lysogenic and lytic growth of Salmonella bacteriophage P22. The solution structure of its C-terminal tetramerization domain, which holds together the two dimeric DNA-binding domains, has been determined by NMR spectroscopy. This structure reveals an assembly of four alpha-helical subunits, consisting of a dimer of two antiparallel coiled coils with a unique right-handed twist. The superhelical winding is considerably stronger and the interhelical separation closer than those found in the well-known left-handed coiled coils in fibrous proteins and leucine zippers. An unusual asymmetry arises between the two monomers that comprise one right-handed coiled coil. A difference in the packing to the adjacent monomer of the other coiled coil occurs with an offset of two helical turns. The two asymmetric monomers within each coiled coil interconvert on a time scale of seconds. Both with respect to symmetry and handedness of helical packing, the C2 symmetric four-helix bundle of Mnt differs from other oligomerization domains that assemble DNA-binding modules, such as that in the tumor suppressor p53 and the E. coli lac repressor.
About this Structure
1QEY is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils., Nooren IM, Kaptein R, Sauer RT, Boelens R, Nat Struct Biol. 1999 Aug;6(8):755-9. PMID:10426954
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