3qpf

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Current revision (10:48, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qpf' size='340' side='right'caption='[[3qpf]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3qpf' size='340' side='right'caption='[[3qpf]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</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>
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<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>
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<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>
<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>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A0H2URZ6_STRPN A0A0H2URZ6_STRPN]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qpf" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Deng, L E]]
 
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[[Category: Gregg, K J]]
 
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[[Category: Hehemann, J H]]
 
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[[Category: Vocadlo, D J]]
 
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[[Category: Whitworth, G E]]
 
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[[Category: Zandberg, W F]]
 
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[[Category: Alpha-alpha six fold]]
 
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[[Category: Glycoside hydrolase]]
 
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[[Category: Hydrolase]]
 
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[[Category: Mannosidase]]
 
[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: Deng LE]]
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[[Category: Gregg KJ]]
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[[Category: Hehemann J-H]]
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[[Category: Vocadlo DJ]]
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[[Category: Whitworth GE]]
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[[Category: Zandberg WF]]

Current revision

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

PDB ID 3qpf

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Proteopedia Page Contributors and Editors (what is this?)

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