6OR4

Crystal structure of SpGH29

Summary for 6OR4

• Entry DOI: 10.2210/pdb6or4/pdb
• Related PRD ID: PRD_900129
• Descriptor: Glycoside hydrolase, beta-D-galactopyranose-(1-3)-[alpha-L-fucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: glycoside hydrolase, hydrolase
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 2
• Total formula weight: 102982.90

Authors

Pluvinage, B.,Boraston, A.B. (deposition date: 2019-04-29, release date: 2019-07-10, Last modification date: 2023-10-11)

Primary citation

Hobbs, J.K.,Pluvinage, B.,Robb, M.,Smith, S.P.,Boraston, A.B.
Two complementary alpha-fucosidases fromStreptococcus pneumoniaepromote complete degradation of host-derived carbohydrate antigens.
J.Biol.Chem., 294:12670-12682, 2019

PubMed Abstract: An important aspect of the interaction between the opportunistic bacterial pathogen and its human host is its ability to harvest host glycans. The pneumococcus can degrade a variety of complex glycans, including - and -linked glycans, glycosaminoglycans, and carbohydrate antigens, an ability that is tightly linked to the virulence of Although is known to use a sophisticated enzyme machinery to attack the human glycome, how it copes with fucosylated glycans, which are primarily histo-blood group antigens, is largely unknown. Here, we identified two pneumococcal enzymes, GH29 and GH95, that target α-(1→3/4) and α-(1→2) fucosidic linkages, respectively. X-ray crystallography studies combined with functional assays revealed that GH29 is specific for the Lewis and Lewis antigen motifs and that GH95 is specific for the H(O)-antigen motif. Together, these enzymes could defucosylate Lewis and Lewis antigens in a complementary fashion. reconstruction of glycan degradation cascades disclosed that the individual or combined activities of these enzymes expose the underlying glycan structure, promoting the complete deconstruction of a glycan that would otherwise be resistant to pneumococcal enzymes. These experiments expand our understanding of the extensive capacity of to process host glycans and the likely roles of α-fucosidases in this. Overall, given the importance of enzymes that initiate glycan breakdown in pneumococcal virulence, such as the neuraminidase NanA and the mannosidase GH92, we anticipate that the α-fucosidases identified here will be important factors in developing more refined models of the -host interaction.

PubMed: 31266803
DOI: 10.1074/jbc.RA119.009368

Experimental method

X-RAY DIFFRACTION (2.1 Å)