5MLT

Structural characterization of a carbohydrate substrate binding protein from Streptococcus pneumoniae

Summary for 5MLT

• Entry DOI: 10.2210/pdb5mlt/pdb
• Descriptor: ABC transporter, substrate-binding protein, ZINC ION (3 entities in total)
• Functional Keywords: substrate binding protein carbohydrate periplasmic binding protein type 2 superfamily, transport protein
• Biological source: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
• Total number of polymer chains: 1
• Total formula weight: 51465.72

Authors

Culurgioni, S.,Tang, M.,Walsh, M.A. (deposition date: 2016-12-07, release date: 2017-01-11, Last modification date: 2024-10-23)

Primary citation

Culurgioni, S.,Tang, M.,Walsh, M.A.
Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.
Acta Crystallogr F Struct Biol Commun, 73:54-61, 2017

PubMed Abstract: Streptococcus pneumoniae is an opportunistic respiratory pathogen that remains a major cause of morbidity and mortality globally, with infants and the elderly at the highest risk. S. pneumoniae relies entirely on carbohydrates as a source of carbon and dedicates a third of all uptake systems to carbohydrate import. The structure of the carbohydrate-free substrate-binding protein SP0092 at 1.61 Å resolution reveals it to belong to the newly proposed subclass G of substrate-binding proteins, with a ligand-binding pocket that is large enough to accommodate complex oligosaccharides. SP0092 is a dimer in solution and the crystal structure reveals a domain-swapped dimer with the monomer subunits in a closed conformation but in the absence of carbohydrate ligand. This closed conformation may be induced by dimer formation and could be used as a mechanism to regulate carbohydrate uptake.

PubMed: 28045395
DOI: 10.1107/S2053230X16020252

Experimental method

X-RAY DIFFRACTION (1.61 Å)