3H72

Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA

Summary for 3H72

• Entry DOI: 10.2210/pdb3h72/pdb
• Related: 3H6J 3H71 3H73
• Descriptor: Sialidase A, N-acetyl-alpha-neuraminic acid (3 entities in total)
• Functional Keywords: six-bladed beta-propeller, cell wall, glycosidase, hydrolase, peptidoglycan-anchor, secreted
• Biological source: Streptococcus pneumoniae
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : P62576
• Total number of polymer chains: 2
• Total formula weight: 107762.35

Authors

Hsiao, Y.-S.,Tong, L. (deposition date: 2009-04-24, release date: 2009-05-12, Last modification date: 2024-02-21)

Primary citation

Hsiao, Y.-S.,Parker, D.,Ratner, A.J.,Prince, A.,Tong, L.
Crystal structures of respiratory pathogen neuraminidases
Biochem.Biophys.Res.Commun., 380:467-471, 2009

PubMed Abstract: Currently there is pressing need to develop novel therapeutic agents for the treatment of infections by the human respiratory pathogens Pseudomonas aeruginosa and Streptococcus pneumoniae. The neuraminidases of these pathogens are important for host colonization in animal models of infection and are attractive targets for drug discovery. To aid in the development of inhibitors against these neuraminidases, we have determined the crystal structures of the P. aeruginosa enzyme NanPs and S. pneumoniae enzyme NanA at 1.6 and 1.7A resolution, respectively. In situ proteolysis with trypsin was essential for the crystallization of our recombinant NanA. The active site regions of the two enzymes are strikingly different. NanA contains a deep pocket that is similar to that in canonical neuraminidases, while the NanPs active site is much more open. The comparative studies suggest that NanPs may not be a classical neuraminidase, and may have distinct natural substrates and physiological functions. This work represents an important step in the development of drugs to prevent respiratory tract colonization by these two pathogens.

PubMed: 19284989
DOI: 10.1016/j.bbrc.2009.01.108

Experimental method

X-RAY DIFFRACTION (1.7 Å)