3FHQ

Structure of endo-beta-N-acetylglucosaminidase A

Summary for 3FHQ

• Entry DOI: 10.2210/pdb3fhq/pdb
• Descriptor: Endo-beta-N-acetylglucosaminidase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose, 3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL, ... (4 entities in total)
• Functional Keywords: endo-a, glycoprotein, man3glcnac-thiazoline, glcnac-asn, glycosidase, hydrolase
• Biological source: Arthrobacter protophormiae
• Total number of polymer chains: 4
• Total formula weight: 281574.32

Authors

Jie, Y.,Li, L.,Shaw, N.,Li, Y.,Song, J.,Zhang, W.,Xia, C.,Zhang, R.,Joachimiak, A.,Zhang, H.-C.,Wang, L.-X.,Wang, P.,Liu, Z.-J. (deposition date: 2008-12-10, release date: 2009-05-05, Last modification date: 2023-11-01)

Primary citation

Yin, J.,Li, L.,Shaw, N.,Li, Y.,Song, J.K.,Zhang, W.,Xia, C.,Zhang, R.,Joachimiak, A.,Zhang, H.-C.,Wang, L.X.,Liu, Z.-J.,Wang, P.
Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A
Plos One, 4:e4658-e4658, 2009

PubMed Abstract: Endo-beta-N-acetylglucosaminidases (ENGases) are dual specificity enzymes with an ability to catalyze hydrolysis and transglycosylation reactions. Recently, these enzymes have become the focus of intense research because of their potential for synthesis of glycopeptides. We have determined the 3D structures of an ENGase from Arthrobacter protophormiae (Endo-A) in 3 forms, one in native form, one in complex with Man(3)GlcNAc-thiazoline and another in complex with GlcNAc-Asn. The carbohydrate moiety sits above the TIM-barrel in a cleft region surrounded by aromatic residues. The conserved essential catalytic residues - E173, N171 and Y205 are within hydrogen bonding distance of the substrate. W216 and W244 regulate access to the active site during transglycosylation by serving as "gate-keepers". Interestingly, Y299F mutation resulted in a 3 fold increase in the transglycosylation activity. The structure provides insights into the catalytic mechanism of GH85 family of glycoside hydrolases at molecular level and could assist rational engineering of ENGases.

PubMed: 19252736
DOI: 10.1371/journal.pone.0004658

Experimental method

X-RAY DIFFRACTION (2.452 Å)