4A4A

CpGH89 (E483Q, E601Q), from Clostridium perfringens, in complex with its substrate GlcNAc-alpha-1,4-galactose

Summary for 4A4A

• Entry DOI: 10.2210/pdb4a4a/pdb
• Related: 2VC9 2VCA 2VCB 2VCC 4A3Z 4A41 4A43 4A44 4A45
• Descriptor: ALPHA-N-ACETYLGLUCOSAMINIDASE FAMILY PROTEIN, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-beta-D-galactopyranose, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, 2 hydrolase, family 89 glycoside hydrolase, mucin, carbohydrate-active enzyme
• Biological source: CLOSTRIDIUM PERFRINGENS
• Total number of polymer chains: 1
• Total formula weight: 106488.38

Authors

Ficko-Blean, E.,Stuart, C.P.,Suits, M.D.,Cid, M.,Tessier, M.,Woods, R.J.,Boraston, A.B. (deposition date: 2011-10-07, release date: 2012-04-04, Last modification date: 2024-05-08)

Primary citation

Ficko-Blean, E.,Boraston, A.B.
Structural analysis of a bacterial exo-alpha-D-N-acetylglucosaminidase in complex with an unusual disaccharide found in class III mucin.
Glycobiology, 22:590-595, 2012

PubMed Abstract: CpGH89 is a family 89 glycoside hydrolase with exo-α-D-N-acetylglucosaminidase activity that is produced by the human and animal pathogen Clostridium perfringens. This enzyme is active on the α-D-GlcpNAc-(1 → 4)-D-Galp motif that is displayed on the class III mucins within the gastric mucosa. Other members of this enzyme family, such as human NAGLU, are active on heparan. A truncated version of CpGH89 was rendered inactive through the mutation of two key catalytic residues, the protein crystallized and its structure determined in complex with α-D-GlcpNAc-(1 → 4)-D-Galp to reveal the molecular details of how this unique disaccharide is recognized by CpGH89. An analysis of this substrate complex not only provides insight into how this enzyme selects for its mucin-presented substrate but also advances our understanding of how its clinically relevant mammalian counterparts are specific for heparan.

PubMed: 22090394
DOI: 10.1093/glycob/cwr165

Experimental method

X-RAY DIFFRACTION (1.9 Å)