PDBsum entry 2yl5

Hydrolase

PDB id: 2yl5

Contents

Protein chains

409 a.a.

Ligands

EDO ×12

Metals

_MG ×10

Waters ×2317

PDB id:

2yl5

Name:

Hydrolase

Title:

Inhibition of the pneumococcal virulence factor strh and molecular insights into n-glycan recognition and hydrolysis

Structure:

Beta-n-acetylhexosaminidase. Chain: a, b, c, d. Fragment: residues 627-1064. Synonym: glycoside hydrolase. Engineered: yes

Source:

Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.15Å R-factor: 0.240 R-free: 0.293

Authors:

B.Pluvinage,M.A.Higgins,D.W.Abbott,C.Robb,A.B.Dalia,L.Deng, J.N.Weiser,T.B.Parsons,A.J.Fairbanks,D.J.Vocadlo,A.B.Boraston

Key ref:

B.Pluvinage et al. (2011). Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis. Structure, 19, 1603-1614. PubMed id: 22078560

Date:

31-May-11 Release date: 14-Sep-11

Protein chains

P49610  (STRH_STRPN) -  Beta-N-acetylhexosaminidase from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

Seq: 1312 a.a.

Struc: 409 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.52 - beta-N-acetylhexosaminidase.
• Reaction: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Structure 19:1603-1614 (2011)

PubMed id: 22078560

Inhibition of the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis.

B.Pluvinage, M.A.Higgins, D.W.Abbott, C.Robb, A.B.Dalia, L.Deng, J.N.Weiser, T.B.Parsons, A.J.Fairbanks, D.J.Vocadlo, A.B.Boraston.

ABSTRACT

The complete degradation of N-linked glycans by the pathogenic bacterium Streptococcus pneumoniae is facilitated by the large multimodular cell wall-attached exo-β-D-N-acetylglucosaminidase StrH. Structural dissection of this virulence factor using X-ray crystallography showed it to have two structurally related glycoside hydrolase family 20 catalytic domains, which displayed the expected specificity for complex N-glycans terminating in N-acetylglucosamine but exhibited unexpected differences in their preferences for the substructures present in these glycans. The structures of the two catalytic domains in complex with unhydrolyzed substrates, including an N-glycan possessing a bisecting N-acetylglucosamine residue, revealed the specific architectural features in the active sites that confer their differential specificities. Inhibitors of StrH are demonstrated to be effective tools in modulating the interaction of StrH with components of the host, such as the innate immune system. Overall, new structural and functional insight into a carbohydrate-mediated component of the pneumococcus-host interaction is provided.