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| | ==Crystal structure of NanS== | | ==Crystal structure of NanS== |
| - | <StructureSection load='3pt5' size='340' side='right' caption='[[3pt5]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3pt5' size='340' side='right'caption='[[3pt5]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3pt5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_0157:h7_edl933 Escherichia coli 0157:h7 edl933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PT5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3pt5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._EDL933 Escherichia coli O157:H7 str. EDL933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PT5 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECs5268, YjhS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155864 Escherichia coli 0157:H7 EDL933])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pt5 OCA], [http://pdbe.org/3pt5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pt5 RCSB], [http://www.ebi.ac.uk/pdbsum/3pt5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pt5 ProSAT]</span></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=3pt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pt5 OCA], [https://pdbe.org/3pt5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pt5 RCSB], [https://www.ebi.ac.uk/pdbsum/3pt5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pt5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A0H3JKI3_ECO57 A0A0H3JKI3_ECO57] |
| - | There is a high prevalence of sialic acid in a number of different organisms, resulting in there being a myriad of different enzymes that can exploit it as a fermentable carbon source. One such enzyme is NanS, a carbohydrate esterase that we show here deacetylates the 9 position of 9-O-sialic acid so that it can be readily transported into the cell for catabolism. Through structural studies we show that NanS adopts a SGNH hydrolase fold. Although the backbone of the structure is similar to previously characterized family members, sequence comparisons indicate that this family can be further subdivided into two subfamilies with somewhat different fingerprints. NanS is the founding member of group II. Its catalytic center contains Ser19 and His301 but no Asp/Glu is present to form the classical catalytic triad. The contribution of Ser19 and His301 to catalysis was confirmed by mutagenesis. In addition to structural characterization we have mapped the specificity of NanS using a battery of substrates.
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| - | Structural and enzymatic characterization of NanS (YjhS), a 9-O-acetyl N-acetylneuraminic acid esterase from escherichia coli O157:H7.,Rangarajan ES, Ruane KM, Proteau A, Schrag JD, Valladares R, Gonzalez CF, Gilbert M, Yakunin AF, Cygler M Protein Sci. 2011 May 6. doi: 10.1002/pro.649. PMID:21557376<ref>PMID:21557376</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3pt5" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli 0157:h7 edl933]] | + | [[Category: Escherichia coli O157:H7 str. EDL933]] |
| - | [[Category: Cygler, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Proteau, A]] | + | [[Category: Cygler M]] |
| - | [[Category: Rangarajan, E S]]
| + | [[Category: Proteau A]] |
| - | [[Category: Ruane, K M]]
| + | [[Category: Rangarajan ES]] |
| - | [[Category: Schrag, J D]] | + | [[Category: Ruane KM]] |
| - | [[Category: 9-o-acetyl n-acetylneuraminic acid esterase]] | + | [[Category: Schrag JD]] |
| - | [[Category: Bsgi]] | + | |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Structural genomic]]
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| - | [[Category: Sgnh hydrolase]]
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