4EPC

Crystal structure of Autolysin repeat domains from Staphylococcus epidermidis

4EPC の概要

• エントリーDOI: 10.2210/pdb4epc/pdb
• 分子名称: N-acetylmuramoyl-L-alanine amidase (2 entities in total)
• 機能のキーワード: sh3b fold, extracellular, hydrolase
• 由来する生物種: Staphylococcus epidermidis
• 細胞内の位置: Secreted: O33635
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36648.05

構造登録者

Zoll, S.,Stehle, T. (登録日: 2012-04-17, 公開日: 2012-06-06, 最終更新日: 2025-03-26)

主引用文献

Zoll, S.,Schlag, M.,Shkumatov, A.V.,Rautenberg, M.,Svergun, D.I.,Gotz, F.,Stehle, T.
Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition.
J.Bacteriol., 194:3789-3802, 2012

PubMed Abstract: The bifunctional major autolysin Atl plays a key role in staphylococcal cell separation. Processing of Atl yields catalytically active amidase (AM) and glucosaminidase (GL) domains that are each fused to repeating units. The two repeats of AM (R1 and R2) target the enzyme to the septum, where it cleaves murein between dividing cells. We have determined the crystal structure of R2, which reveals that each repeat folds into two half-open β-barrel subunits. We further demonstrate that lipoteichoic acid serves as a receptor for the repeats and that this interaction depends on conserved surfaces in each subunit. Small-angle X-ray scattering of the mature amidase reveals the presence of flexible linkers separating the AM, R1, and R2 units. Different levels of flexibility for each linker provide mechanistic insights into the conformational dynamics of the full-length protein and the roles of its components in cell wall association and catalysis. Our analysis supports a model in which the repeats direct the catalytic AM domain to the septum, where it can optimally perform the final step of cell division.

PubMed: 22609916
DOI: 10.1128/JB.00331-12

実験手法

X-RAY DIFFRACTION (2.9 Å)