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3qt9
From Proteopedia
(Difference between revisions)
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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, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose== | |
| - | + | <StructureSection load='3qt9' size='340' side='right' caption='[[3qt9]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3qt9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QT9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=YDR:6-S-ALPHA-D-MANNOPYRANOSYL-6-THIO-ALPHA-D-MANNOPYRANOSE'>YDR</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qt3|3qt3]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPE0426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 Clostridium perfringens])</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=3qt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qt9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qt9 RCSB], [http://www.ebi.ac.uk/pdbsum/3qt9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
| - | [[Category: Boraston, A B | + | [[Category: Boraston, A B]] |
| - | [[Category: Deng, L E | + | [[Category: Deng, L E]] |
| - | [[Category: Gregg, K J | + | [[Category: Gregg, K J]] |
| - | [[Category: Hehemann, J H | + | [[Category: Hehemann, J H]] |
| - | [[Category: Vocadlo, D J | + | [[Category: Vocadlo, D J]] |
| - | [[Category: Whitworth, G E | + | [[Category: Whitworth, G E]] |
| - | [[Category: Zandberg, W F | + | [[Category: Zandberg, W F]] |
[[Category: Alpha-alpha six fold]] | [[Category: Alpha-alpha six fold]] | ||
[[Category: Glycoside hydrolase]] | [[Category: Glycoside hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mannosidase]] | [[Category: Mannosidase]] | ||
Revision as of 10:54, 19 December 2014
Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose
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