5KZD

N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus with bound sialic acid alditol

5KZD の概要

• エントリーDOI: 10.2210/pdb5kzd/pdb
• 関連するPDBエントリー: 5KZE
• 分子名称: 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)
• 機能のキーワード: tim-barrel, inhibitor, n-acetylneuraminate lyase, lyase
• 由来する生物種: Staphylococcus aureus (strain USA300)
• 細胞内の位置: Cytoplasm : Q2FJU9
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 133551.00

構造登録者

North, R.A.,Watson, A.J.A.,Pearce, F.G.,Muscroft-Taylor, A.C.,Friemann, R.,Fairbanks, A.J.,Dobson, R.C.J. (登録日: 2016-07-25, 公開日: 2017-01-11, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.334 Å)