1qey
From Proteopedia
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| - | [[Image:1qey.gif|left|200px]] | ||
| - | + | ==NMR Structure Determination of the Tetramerization Domain of the MNT Repressor: An Asymmetric A-Helical Assembly in Slow Exchange== | |
| - | + | <StructureSection load='1qey' size='340' side='right'caption='[[1qey]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1qey]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QEY FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qey OCA], [https://pdbe.org/1qey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qey RCSB], [https://www.ebi.ac.uk/pdbsum/1qey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qey ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/RMNT_BPP22 RMNT_BPP22] Mnt acts as a transcriptional repressor of genes ant and arc. | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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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. | 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. | ||
| - | + | 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<ref>PMID:10426954</ref> | |
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| - | The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils., Nooren IM, Kaptein R, Sauer RT, Boelens R | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1qey" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Salmonella virus P22]] | ||
| + | [[Category: Boelens R]] | ||
| + | [[Category: George AVE]] | ||
| + | [[Category: Kaptein R]] | ||
| + | [[Category: Nooren IMA]] | ||
| + | [[Category: Sauer RT]] | ||
Current revision
NMR Structure Determination of the Tetramerization Domain of the MNT Repressor: An Asymmetric A-Helical Assembly in Slow Exchange
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