This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2uvk
From Proteopedia
(Difference between revisions)
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2uvk.jpg|left|200px]] | ||
| - | + | ==Structure of YjhT== | |
| - | + | <StructureSection load='2uvk' size='340' side='right'caption='[[2uvk]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[2uvk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecobb Ecobb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UVK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UVK FirstGlance]. <br> |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=2uvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uvk OCA], [https://pdbe.org/2uvk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uvk RCSB], [https://www.ebi.ac.uk/pdbsum/2uvk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uvk ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [[https://www.uniprot.org/uniprot/NANM_ECOLI NANM_ECOLI]] Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.<ref>PMID:18063573</ref> | |
| - | + | == 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/uv/2uvk_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2uvk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The acquisition of host-derived sialic acid is an important virulence factor for some bacterial pathogens, but in vivo this sugar acid is sequestered in sialoconjugates as the alpha-anomer. In solution, however, sialic acid is present mainly as the beta-anomer, formed by a slow spontaneous mutarotation. We studied the Escherichia coli protein YjhT as a member of a family of uncharacterized proteins present in many sialic acid-utilizing pathogens. This protein is able to accelerate the equilibration of the alpha- and beta-anomers of the sialic acid N-acetylneuraminic acid, thus describing a novel sialic acid mutarotase activity. The structure of this periplasmic protein, solved to 1.5A resolution, reveals a dimeric 6-bladed unclosed beta-propeller, the first of a bacterial Kelch domain protein. Mutagenesis of conserved residues in YjhT demonstrated an important role for Glu-209 and Arg-215 in mutarotase activity. We also present data suggesting that the ability to utilize alpha-N-acetylneuraminic acid released from complex sialoconjugates in vivo provides a physiological advantage to bacteria containing YjhT. | ||
| - | + | Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT.,Severi E, Muller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH J Biol Chem. 2008 Feb 22;283(8):4841-9. Epub 2007 Dec 5. PMID:18063573<ref>PMID:18063573</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2uvk" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Muller, A | + | __TOC__ |
| - | [[Category: Severi, E | + | </StructureSection> |
| - | [[Category: Thomas, G H | + | [[Category: Ecobb]] |
| - | [[Category: Wilson, K S | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Muller, A]] |
| - | [[Category: | + | [[Category: Severi, E]] |
| - | + | [[Category: Thomas, G H]] | |
| - | [[Category: | + | [[Category: Wilson, K S]] |
| - | [[Category: | + | [[Category: Beta-propeller]] |
| - | [[Category: | + | [[Category: Hypothetical protein]] |
| - | + | [[Category: Kelch repeat]] | |
| - | + | [[Category: Sialic acid metabolism]] | |
| + | [[Category: Unknown function]] | ||
Current revision
Structure of YjhT
| |||||||||||
