1irq: Difference between revisions
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==Crystal structure of omega transcriptional repressor at 1.5A resolution== | ==Crystal structure of omega transcriptional repressor at 1.5A resolution== | ||
<StructureSection load='1irq' size='340' side='right' caption='[[1irq]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1irq' size='340' side='right'caption='[[1irq]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1irq]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1irq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRQ FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=1irq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irq OCA], [https://pdbe.org/1irq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1irq RCSB], [https://www.ebi.ac.uk/pdbsum/1irq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1irq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q57468_STRPY Q57468_STRPY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Alonso | [[Category: Streptococcus pyogenes]] | ||
[[Category: | [[Category: Alonso JC]] | ||
[[Category: Murayama | [[Category: De La Hoz AB]] | ||
[[Category: Orth | [[Category: Murayama K]] | ||
[[Category: Saenger | [[Category: Orth P]] | ||
[[Category: Saenger W]] | |||
Latest revision as of 02:35, 28 December 2023
Crystal structure of omega transcriptional repressor at 1.5A resolutionCrystal structure of omega transcriptional repressor at 1.5A resolution
Structural highlights
FunctionPublication Abstract from PubMedThe 71 amino acid residue omega protein encoded by the Streptococcus pyogenes non-conjugative plasmid pSM19035 is a transcriptional repressor that regulates expression of genes for copy number control and stable maintenance of plasmids. The crystal structure of omega protein has been determined by multiple isomorphous replacement, including anomalous scattering and refined to an R-factor of 21.1 % (R(free)=23.2 %) at 1.5 A resolution. Two monomers related by a non-crystallographic 2-fold axis form a homodimer that occupies the asymmetric unit. Each polypeptide chain is folded into two alpha-helices and one beta-strand forming an antiparallel beta-ribbon in the homodimer. The N-terminal regions (1-23 and 1-22 in subunits I and II, respectively) are not defined in the electron density due to proteolysis of the N-terminal 20 amino acid residues during crystallisation and partial disorder. The omega protein belongs to the structural superfamily of MetJ/Arc repressors featuring a ribbon-helix-helix DNA-binding motif with the beta-ribbon located in and recognizing the major groove of operator DNA; according to a modelled omega protein-DNA complex, residues Arg31 and Arg31' on the beta-ribbon are in positions to interact with a nucleobase, especially guanine. Crystal structure of omega transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 A resolution.,Murayama K, Orth P, de la Hoz AB, Alonso JC, Saenger W J Mol Biol. 2001 Dec 7;314(4):789-96. PMID:11733997[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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