2h1t
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2h1t" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h1t, resolution 1.800Å" /> '''Crystal structure o...) |
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| - | [[Image:2h1t.gif|left|200px]]<br /><applet load="2h1t" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2h1t, resolution 1.800Å" /> | ||
| - | '''Crystal structure of a protein of unknown function from DUF1089 family (NP_250684.1) from Pseudomonas aeruginosa at 1.80 A resolution'''<br /> | ||
| - | == | + | ==Crystal structure of a duf1089 family protein (pa1994) from pseudomonas aeruginosa at 1.80 A resolution== |
| - | + | <StructureSection load='2h1t' size='340' side='right'caption='[[2h1t]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [ | + | <table><tr><td colspan='2'>[[2h1t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1T 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]] 1.8Å</td></tr> |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=2h1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1t OCA], [https://pdbe.org/2h1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1t RCSB], [https://www.ebi.ac.uk/pdbsum/2h1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1t ProSAT], [https://www.topsan.org/Proteins/JCSG/2h1t TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | [[ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/Q9I2B5_PSEAE Q9I2B5_PSEAE] |
| - | [[ | + | == 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/h1/2h1t_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=2h1t ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The crystal structure of PA1994 from Pseudomonas aeruginosa, a member of the Pfam PF06475 family classified as a domain of unknown function (DUF1089), reveals a novel fold comprising a 15-stranded beta-sheet wrapped around a single alpha-helix that assembles into a tight dimeric arrangement. The remote structural similarity to lipoprotein localization factors, in addition to the presence of an acidic pocket that is conserved in DUF1089 homologs, phospholipid-binding and sugar-binding proteins, indicate a role for PA1994 and the DUF1089 family in glycolipid metabolism. Genome-context analysis lends further support to the involvement of this family of proteins in glycolipid metabolism and indicates possible activation of DUF1089 homologs under conditions of bacterial cell-wall stress or host-pathogen interactions. | ||
| - | + | The structure of the first representative of Pfam family PF06475 reveals a new fold with possible involvement in glycolipid metabolism.,Bakolitsa C, Kumar A, McMullan D, Krishna SS, Miller MD, Carlton D, Najmanovich R, Abdubek P, Astakhova T, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Feuerhelm J, Grant JC, Grzechnik SK, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Marciano D, Morse AT, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Trout CV, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Wilson IA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt, 10):1211-7. Epub 2009 Oct 27. PMID:20944213<ref>PMID:20944213</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2h1t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
Current revision
Crystal structure of a duf1089 family protein (pa1994) from pseudomonas aeruginosa at 1.80 A resolution
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