5KZE

N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus

Summary for 5KZE

• Entry DOI: 10.2210/pdb5kze/pdb
• Related: 5KZD
• Descriptor: N-acetylneuraminate lyase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tim-barrel, n-acetylneuraminate lyase, lyase
• Biological source: Staphylococcus aureus (strain USA300)
• Cellular location: Cytoplasm : Q2FJU9
• Total number of polymer chains: 8
• Total formula weight: 266116.98

Authors

North, R.A.,Watson, A.J.A.,Pearce, F.G.,Muscroft-Taylor, A.C.,Friemann, R.,Fairbanks, A.J.,Dobson, R.C.J. (deposition date: 2016-07-25, release date: 2017-01-11, Last modification date: 2023-10-04)

Primary citation

North, R.A.,Watson, A.J.,Pearce, F.G.,Muscroft-Taylor, A.C.,Friemann, R.,Fairbanks, A.J.,Dobson, R.C.
Structure and inhibition of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.
FEBS Lett., 590:4414-4428, 2016

PubMed Abstract: N-Acetylneuraminate lyase is the first committed enzyme in the degradation of sialic acid by bacterial pathogens. In this study, we analyzed the kinetic parameters of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus (MRSA). We determined that the enzyme has a relatively high K of 3.2 mm, suggesting that flux through the catabolic pathway is likely to be controlled by this enzyme. Our data indicate that sialic acid alditol, a known inhibitor of N-acetylneuraminate lyase enzymes, is a stronger inhibitor of MRSA N-acetylneuraminate lyase than of Clostridium perfringens N-acetylneuraminate lyase. Our analysis of the crystal structure of ligand-free and 2R-sialic acid alditol-bound MRSA N-acetylneuraminate lyase suggests that subtle dynamic differences in solution and/or altered binding interactions within the active site may account for species-specific inhibition.

PubMed: 27943302
DOI: 10.1002/1873-3468.12462

Experimental method

X-RAY DIFFRACTION (1.74 Å)