1AMX

COLLAGEN-BINDING DOMAIN FROM A STAPHYLOCOCCUS AUREUS ADHESIN

1AMX の概要

• エントリーDOI: 10.2210/pdb1amx/pdb
• 分子名称: COLLAGEN ADHESIN (2 entities in total)
• 機能のキーワード: bacterial adhesin, mscramm
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q53654
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20314.10

構造登録者

Symersky, J.,Narayana, S. (登録日: 1997-06-19, 公開日: 1998-06-24, 最終更新日: 2024-02-07)

主引用文献

Symersky, J.,Patti, J.M.,Carson, M.,House-Pompeo, K.,Teale, M.,Moore, D.,Jin, L.,Schneider, A.,DeLucas, L.J.,Hook, M.,Narayana, S.V.
Structure of the collagen-binding domain from a Staphylococcus aureus adhesin.
Nat.Struct.Biol., 4:833-838, 1997

PubMed Abstract: The crystal structure of the recombinant 19,000 M(r) binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 A resolution. The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on beta-sheet I exhibited the best surface complementarity to the collagen probes. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen. Here we present a structural perspective for the mode of collagen binding by a bacterial surface protein.

PubMed: 9334749
DOI: 10.1038/nsb1097-833

実験手法

X-RAY DIFFRACTION (2 Å)