1qey

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1qey" [edit=sysop:move=sysop])
Line 1: Line 1:
-
[[Image:1qey.png|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]], [[NMR_Ensembles_of_Models | 27 NMR models]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1qey]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QEY FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qey OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qey RCSB], [http://www.ebi.ac.uk/pdbsum/1qey PDBsum]</span></td></tr>
 +
<table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
{{STRUCTURE_1qey| PDB=1qey | SCENE= }}
+
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>
-
===NMR Structure Determination of the Tetramerization Domain of the MNT Repressor: An Asymmetric A-Helical Assembly in Slow Exchange===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_10426954}}
+
== References ==
-
 
+
<references/>
-
==About this Structure==
+
__TOC__
-
[[1qey]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QEY OCA].
+
</StructureSection>
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:010426954</ref><references group="xtra"/>
+
[[Category: Enterobacteria phage p22]]
[[Category: Enterobacteria phage p22]]
[[Category: Boelens, R.]]
[[Category: Boelens, R.]]

Revision as of 07:02, 9 June 2014

NMR Structure Determination of the Tetramerization Domain of the MNT Repressor: An Asymmetric A-Helical Assembly in Slow Exchange

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qey"
Views
Personal tools
Navigation
Toolbox