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3qpf

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Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure

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 <StructureSection load='3qpf' size='340' side='right'caption='[[3qpf]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qpf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qpf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QPF FirstGlance]. <br>
-</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></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]] 2.15&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SP_2144 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</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></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=3qpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qpf OCA], [https://pdbe.org/3qpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qpf RCSB], [https://www.ebi.ac.uk/pdbsum/3qpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qpf ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A0H2URZ6_STRPN A0A0H2URZ6_STRPN]
-The modification of N-glycans by alpha-mannosidases is a process that is relevant to a large number of biologically important processes, including infection by microbial pathogens and colonization by microbial symbionts. At present, described mannosidases that are specific for alpha-1,6-mannose linkages are very limited in number. Through structural and functional analysis of two sequence related enzymes, one from Streptococcus pneumoniae (SpGHX) and one from Clostridium perfringens (CpGHX), a new glycoside hydrolase family, GHX, is identified and characterized. Analysis of SpGHX and CpGHX reveal them to have exo-alpha-1,6-mannosidase activity consistent with specificity for N-linked glycans having their alpha-1,3-mannose branches removed. The X-ray crystal structures of SpGHX and CpGHX obtained in apo-, inhibitor bound, and substrate bound forms provide both mechanistic and molecular insight into how these proteins, which adopt an (alpha/alpha)6-fold, recognize and hydrolyze the alpha-1,6-mannosidic bond by an inverting, metal-independent catalytic mechanism. A phylogenetic analysis of GHX proteins reveals this to be a relatively large and widespread family found frequently in bacterial pathogens, bacterial human gut symbionts, and a variety of fungi. Based on these studies we predict this family of enzymes will primarily comprise such exo-alpha-1,6-mannosidases.
-Analysis of new family of widely distributed metal-independent {alpha}-mannosidases provides unique insight into the processing of N-linked glycans.,Gregg KJ, Zandberg WF, Hehemann JH, Whitworth GE, Deng L, Vocadlo DJ, Boraston AB J Biol Chem. 2011 Mar 9. PMID:21388958<ref>PMID:21388958</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3qpf" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Deng, L E]]
-[[Category: Gregg, K J]]
-[[Category: Hehemann, J H]]
-[[Category: Vocadlo, D J]]
-[[Category: Whitworth, G E]]
-[[Category: Zandberg, W F]]
-[[Category: Alpha-alpha six fold]]
-[[Category: Glycoside hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Mannosidase]]
 [[Category: Streptococcus pneumoniae]]
+[[Category: Deng LE]]
+[[Category: Gregg KJ]]
+[[Category: Hehemann J-H]]
+[[Category: Vocadlo DJ]]
+[[Category: Whitworth GE]]
+[[Category: Zandberg WF]]

3qpf

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Analysis of a New Family of Widely Distributed Metal-independent alpha-Mannosidases Provides Unique Insight into the Processing of N-linked Glycans, Streptococcus pneumoniae SP_2144 apo-structure

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