5KZD
N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol
Summary for 5KZD
| Entry DOI | 10.2210/pdb5kzd/pdb |
| Related | 5KZE |
| Descriptor | N-acetylneuraminate lyase, (2~{S},4~{S},5~{R},6~{R},7~{S},8~{R})-5-acetamido-2,4,6,7,8,9-hexakis(oxidanyl)nonanoic acid (3 entities in total) |
| Functional Keywords | tim-barrel, inhibitor, n-acetylneuraminate lyase, lyase |
| Biological source | Staphylococcus aureus (strain USA300) |
| Cellular location | Cytoplasm : Q2FJU9 |
| Total number of polymer chains | 4 |
| Total formula weight | 133551.00 |
| 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: 2024-03-06) |
| 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 Cited by 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: 27943302DOI: 10.1002/1873-3468.12462 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.334 Å) |
Structure validation
Download full validation report
