2WYH

Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase

Summary for 2WYH

• Entry DOI: 10.2210/pdb2wyh/pdb
• Related: 2WYI
• Descriptor: ALPHA-MANNOSIDASE, ZINC ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: hydrolase, glycosidase, glycoside hydrolase
• Biological source: STREPTOCOCCUS PYOGENES
• Total number of polymer chains: 2
• Total formula weight: 211841.40

Authors

Suits, M.D.L.,Zhu, Y.,Taylor, E.J.,Zechel, D.L.,Gilbert, H.J.,Davies, G.J. (deposition date: 2009-11-16, release date: 2010-02-16, Last modification date: 2024-05-08)

Primary citation

Suits, M.D.L.,Zhu, Y.,Taylor, E.J.,Zechel, D.L.,Gilbert, H.J.,Davies, G.J.
Structure and Kinetic Investigation of Streptococcus Pyogenes Family Gh38 Alpha-Mannosidase
Plos One, 5:E9006-, 2010

PubMed Abstract: The enzymatic hydrolysis of alpha-mannosides is catalyzed by glycoside hydrolases (GH), termed alpha-mannosidases. These enzymes are found in different GH sequence-based families. Considerable research has probed the role of higher eukaryotic "GH38" alpha-mannosides that play a key role in the modification and diversification of hybrid N-glycans; processes with strong cellular links to cancer and autoimmune disease. The most extensively studied of these enzymes is the Drosophila GH38 alpha-mannosidase II, which has been shown to be a retaining alpha-mannosidase that targets both alpha-1,3 and alpha-1,6 mannosyl linkages, an activity that enables the enzyme to process GlcNAc(Man)(5)(GlcNAc)(2) hybrid N-glycans to GlcNAc(Man)(3)(GlcNAc)(2). Far less well understood is the observation that many bacterial species, predominantly but not exclusively pathogens and symbionts, also possess putative GH38 alpha-mannosidases whose activity and specificity is unknown.

PubMed: 20140249
DOI: 10.1371/JOURNAL.PONE.0009006

Experimental method

X-RAY DIFFRACTION (1.9 Å)