2LTJ

Conformational analysis of StrH, the surface-attached exo- beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae

Summary for 2LTJ

• Entry DOI: 10.2210/pdb2ltj/pdb
• NMR Information: BMRB: 18484
• Descriptor: Beta-N-acetylhexosaminidase (1 entity in total)
• Functional Keywords: elongated, b-sheet, hydrolase
• Biological source: Streptococcus pneumoniae
• Cellular location: Secreted, cell wall; Peptidoglycan-anchor (Potential): P49610
• Total number of polymer chains: 1
• Total formula weight: 12292.64

Authors

Pluvinage, B.,Chitayat, S.,Ficko-Blean, E.,Abbott, D.,Kunjachen, J.,Grondin, J.,Spencer, H.,Smith, S.,Boraston, A. (deposition date: 2012-05-28, release date: 2012-11-28, Last modification date: 2024-05-01)

Primary citation

Pluvinage, B.,Chitayat, S.,Ficko-Blean, E.,Abbott, D.W.,Kunjachen, J.M.,Grondin, J.,Spencer, H.L.,Smith, S.P.,Boraston, A.B.
Conformational analysis of StrH, the surface-attached exo-beta-D-N-acetylglucosaminidase from Streptococcus pneumoniae.
J.Mol.Biol., 425:334-349, 2013

PubMed Abstract: Streptococcus pneumoniae is a serious human pathogen that presents on its surface numerous proteins involved in the host-bacterium interaction. The carbohydrate-active enzymes are particularly well represented among these surface proteins, and many of these are known virulence factors, highlighting the importance of carbohydrate processing by this pathogen. StrH is a surface-attached exo-β-D-N-acetylglucosaminidase that cooperates with the sialidase NanA and the β-galactosidase BgaA to sequentially degrade the nonreducing terminal arms of complex N-linked glycans. This enzyme is a large multi-modular protein that is notable for its tandem N-terminal family GH20 catalytic modules, whose individual X-ray crystal structures were recently reported. StrH also contains C-terminal tandem G5 modules, which are uncharacterized. Here, we report the NMR-determined solution structure of the first G5 module in the tandem, G5-1, which along with the X-ray crystal structures of the GH20 modules was used in conjunction with small-angle X-ray scattering to construct a pseudo-atomic model of full-length StrH. The results reveal a model in which StrH adopts an elongated conformation that may project the catalytic modules away from the surface of the bacterium to a distance of up to ~250 Å.

PubMed: 23154168
DOI: 10.1016/j.jmb.2012.11.005

Experimental method

SOLUTION NMR