3c8g: Difference between revisions
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New page: left|200px<br /><applet load="3c8g" size="350" color="white" frame="true" align="right" spinBox="true" caption="3c8g, resolution 2.50Å" /> '''Crystal structure of... |
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== | ==Crystal structure of a possible transciptional regulator YggD from Shigella flexneri 2a str. 2457T== | ||
<StructureSection load='3c8g' size='340' side='right'caption='[[3c8g]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3c8g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri_2a_str._2457T Shigella flexneri 2a str. 2457T]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C8G FirstGlance]. <br> | |||
[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3c8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c8g OCA], [https://pdbe.org/3c8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c8g RCSB], [https://www.ebi.ac.uk/pdbsum/3c8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c8g ProSAT], [https://www.topsan.org/Proteins/MCSG/3c8g TOPSAN]</span></td></tr> | ||
[ | </table> | ||
== Function == | |||
[ | [https://www.uniprot.org/uniprot/FUME_SHIFL FUME_SHIFL] In vitro catalyzes the addition of water to fumarate, forming malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer maleate as substrate.[UniProtKB:P11663] | ||
[[ | == Evolutionary Conservation == | ||
[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[ | Check<jmol> | ||
[ | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c8/3c8g_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3c8g ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Many bacteria express phosphoenolpyruvate-dependent phosphotransferase systems (PTS). The mannitol-specific PTS catalyze the uptake and phosphorylation of d-mannitol. The uptake system comprises several genes encoded in the single operon. The expression of the mannitol operon is regulated by a proposed transcriptional factor, mannitol operon repressor (MtlR) that was first studied in Escherichia coli. Here we report the first crystal structures of MtlR from Vibrio parahemeolyticus (Vp-MtlR) and its homolog YggD protein from Shigella flexneri (Sf-YggD). MtlR and YggD belong to the same protein family (Pfam05068). Although Vp-MtlR and Sf-YggD share low sequence identity (22%), their overall structures are very similar, representing a novel all alpha-helical fold, and indicate similar function. However, their lack of any known DNA-binding structural motifs and their unfavorable electrostatic properties imply that MtlR/YggD are unlikely to bind a specific DNA operator directly as proposed earlier. This structural observation is further corroborated by in vitro DNA-binding studies of E. coli MtlR (Ec-MtlR), which detected no interaction of Ec-MtlR with the well characterized mannitol operator/promoter region. Therefore, MtlR/YggD belongs to a new class of transcription factors in bacteria that may regulate gene expression indirectly as a part of a larger transcriptional complex. | |||
The mannitol operon repressor MtlR belongs to a new class of transcription regulators in bacteria.,Tan K, Clancy S, Borovilos M, Zhou M, Horer S, Moy S, Volkart LL, Sassoon J, Baumann U, Joachimiak A J Biol Chem. 2009 Dec 25;284(52):36670-9. Epub 2009 Oct 19. PMID:19840941<ref>PMID:19840941</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3c8g" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shigella flexneri 2a str. 2457T]] | |||
[[Category: Borovilos M]] | |||
[[Category: Clancy S]] | |||
[[Category: Joachimiak A]] | |||
[[Category: Tan K]] | |||
Latest revision as of 22:32, 26 March 2025
Crystal structure of a possible transciptional regulator YggD from Shigella flexneri 2a str. 2457T
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