3DWK

Identification of Dynamic Structural Motifs Involved in Peptidoglycan Glycosyltransfer

3DWK の概要

• エントリーDOI: 10.2210/pdb3dwk/pdb
• 関連するPDBエントリー: 2OLU 2OLV
• 分子名称: Penicillin-binding protein 2, SULFATE ION, LAURYL DIMETHYLAMINE-N-OXIDE (3 entities in total)
• 機能のキーワード: lysozyme-fold transpeptidase fold pi-helix, cell shape, cell wall biogenesis/degradation, membrane, peptidoglycan synthesis, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 283155.96

構造登録者

Lovering, A.L.,De Castro, L.,Strynadka, N.C.J. (登録日: 2008-07-22, 公開日: 2008-09-30, 最終更新日: 2023-08-30)

主引用文献

Lovering, A.L.,De Castro, L.,Strynadka, N.C.
Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer.
J.Mol.Biol., 383:167-177, 2008

PubMed Abstract: We have determined the structure of a new form of the bifunctional peptidoglycan glycosyltransferase (GT)/transpeptidase penicillin-binding protein 2 from the pathogen Staphylococcus aureus. We observe several previously unstructured regions of the GT substrate-binding pockets, including a pi-bulge in the outer helix that may be responsible for the conformational flexibility of active-site motifs required for transfer of product to the donor binding site during processive rounds of peptidoglycan polymerization. The identification of a beta-hairpin in the usually unstructured region of the fold shares local structural homology to that of an exomuramidase, heightening comparisons between this biosynthetic enzyme and lytic peptidoglycan transglycosylases. This new form also shows remarkable interdomain flexibility, causing the linker region of the fold to project into the GT active site. This self-interaction may have significant consequences for the regulation of polymerization activity. The derived information is used to build a catalytic model of both donor and acceptor glycolipid substrates.

PubMed: 18760285
DOI: 10.1016/j.jmb.2008.08.020

実験手法

X-RAY DIFFRACTION (3.1 Å)