5yyb

Crystal structure of Sialic acid Binding protein from Haemophilus ducreyi with Neu5Gc

spinqualitylabelsall models 5yyb, resolution 2.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5yyb is a 2 chain structure with sequence from Haemophilus ducreyi 35000HP. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.484Å Ligands: MSE, NGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7VL18_HAEDU Publication Abstract from PubMed The primary role of bacterial periplasmic binding proteins is sequestration of essential metabolites present at a low concentration in the periplasm and making them available for active transporters that transfer these ligands into the bacterial cell. The periplasmic binding proteins(SiaP) from the tripartite ATP-independent periplasmic (TRAP) transport system that transports mammalian host-derived sialic acids, have been well studied from different pathogenic bacteria, including Haemophilus influenzae, Fusobacterium nucleatum, Pasteurella multocida, and Vibrio cholerae SiaPs bind the sialic acid N-acetylneuraminic acid (Neu5Ac) with nanomolar affinity by forming electrostatic and hydrogen bonding interactions. Here, we report the crystal structure of a periplasmic binding protein (SatA) of the ATP-binding cassette (ABC) transport system from the pathogenic bacterium Haemophilus ducreyi The structure of Hd-SatA in the native form and sialic acid-bound forms (with Neu5Ac and N-glycolylneuraminic acid [Neu5Gc]), determined to 2.2, 1.5 and 2.5 A resolutions respectively, revealed a ligand-binding site that is very different from those of the SiaPs of the TRAP transport system. A structural comparison along with thermodynamic studies suggested that similar affinities are achieved in the two classes of proteins through distinct mechanisms, one enthalpically driven and the other entropically driven. In summary, our structural and thermodynamic characterization of Hd-SatA reveal that it binds sialic acids with nanomolar affinity and this binding is an entropically driven process. This information is important for future structure-based drug design against this pathogen and related bacteria. Molecular characterization of the interaction of sialic acid with the periplasmic binding protein from Haemophilus ducreyi.,Setty TG, Mowers JC, Hobbs AG, Maiya SP, Syed S, Munson RS Jr, Apicella MA, Subramanian R J Biol Chem. 2018 Oct 12. pii: RA118.005151. doi: 10.1074/jbc.RA118.005151. PMID:30315109 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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