3jqy
From Proteopedia
(Difference between revisions)
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<StructureSection load='3jqy' size='340' side='right'caption='[[3jqy]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3jqy' size='340' side='right'caption='[[3jqy]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3jqy]] is a 3 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3jqy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JQY FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.699Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3jqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jqy OCA], [https://pdbe.org/3jqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jqy RCSB], [https://www.ebi.ac.uk/pdbsum/3jqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jqy ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NEUO_ECOK1 NEUO_ECOK1] Catalyzes the O-acetylation of capsular polymeric sialic acid. Shows high substrate specificity toward polymers of sialic acid that contains a large number of residues.<ref>PMID:15809431</ref> <ref>PMID:17519228</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3jqy ConSurf]. | </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=3jqy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The major virulence factor of the neuroinvasive pathogen Escherichia coli K1 is the K1 capsule composed of alpha2,8-linked polysialic acid (polySia). K1 strains harboring the CUS-3 prophage modify their capsular polysaccharide by phase-variable O-acetylation, a step that is associated with increased virulence. Here we present the crystal structure of the prophage-encoded polysialate O-acetyltransferase NeuO. The homotrimeric enzyme belongs to the left-handed beta-helix (LbetaH) family of acyltransferases and is characterized by an unusual funnel-shaped outline. Comparison with other members of the LbetaH family allowed the identification of active site residues and proposal of a catalytic mechanism and highlighted structural characteristics of polySia specific O-acetyltransferases. As a unique feature of NeuO, the enzymatic activity linearly increases with the length of the N-terminal poly-psi-domain which is composed of a variable number of tandem copies of an RLKTQDS heptad. Since the poly-psi-domain was not resolved in the crystal structure it is assumed to be unfolded in the apo-enzyme. | ||
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| - | Crystal structure analysis of the polysialic acid specific O-acetyltransferase NeuO.,Schulz EC, Bergfeld AK, Ficner R, Muhlenhoff M PLoS One. 2011 Mar 1;6(3):e17403. PMID:21390252<ref>PMID:21390252</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3jqy" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Bergfeld A]] | |
| - | [[Category: Bergfeld | + | [[Category: Ficner R]] |
| - | [[Category: Ficner | + | [[Category: Muehlenhoff M]] |
| - | [[Category: Muehlenhoff | + | [[Category: Schulz E-C]] |
| - | [[Category: Schulz | + | |
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Current revision
Crystal Structure of the polySia specific acetyltransferase NeuO
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