4C1X

Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 6'-sialyllactose

Summary for 4C1X

• Entry DOI: 10.2210/pdb4c1x/pdb
• Related: 4C1W
• Related PRD ID: PRD_900066
• Descriptor: SIALIDASE A, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: hydrolase, sialic acid binding
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : P62575
• Total number of polymer chains: 1
• Total formula weight: 21822.36

Authors

Yang, L.,Connaris, H.,Potter, J.A.,Taylor, G.L. (deposition date: 2013-08-14, release date: 2014-09-10, Last modification date: 2024-05-08)

Primary citation

Yang, L.,Connaris, H.,Potter, J.A.,Taylor, G.L.
Structural Characterization of the Carbohydrate-Binding Module of Nana Sialidase, a Pneumococcal Virulence Factor.
Bmc Struct.Biol., 15:15-, 2015

PubMed Abstract: Streptococcus pneumoniae Neuraminidase A (NanA) is a multi-domain protein anchored to the bacterial surface. Upstream of the catalytic domain of NanA is a domain that conforms to the sialic acid-recognising CBM40 family of the CAZY (carbohydrate-active enzymes) database. This domain has been identified to play a critical role in allowing the bacterium to promote adhesion and invasion of human brain microvascular endothelial cells, and hence may play a key role in promoting bacterial meningitis. In addition, the CBM40 domain has also been reported to activate host chemokines and neutrophil recruitment during infection.

PubMed: 26289431
DOI: 10.1186/S12900-015-0042-4

Experimental method

X-RAY DIFFRACTION (1.84 Å)