6E8M

Legionella Longbeachae LeSH (Llo2327) bound to the human DnaJ-A1 pTyr381 peptide

6E8M の概要

• エントリーDOI: 10.2210/pdb6e8m/pdb
• 分子名称: LeSH (Llo2327), DnaJ-A1 pTyr381 peptide (3 entities in total)
• 機能のキーワード: src homology 2 domain, peptide binding protein
• 由来する生物種: Legionella longbeachae serogroup 1 (strain NSW150); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21470.40

構造登録者

Kaneko, T.,Li, S.S.C. (登録日: 2018-07-30, 公開日: 2018-11-14, 最終更新日: 2024-10-16)

主引用文献

Kaneko, T.,Stogios, P.J.,Ruan, X.,Voss, C.,Evdokimova, E.,Skarina, T.,Chung, A.,Liu, X.,Li, L.,Savchenko, A.,Ensminger, A.W.,Li, S.S.
Identification and characterization of a large family of superbinding bacterial SH2 domains.
Nat Commun, 9:4549-4549, 2018

PubMed Abstract: Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). Apart from a few isolated cases in viruses, no functional SH2 domain has been identified to date in prokaryotes. Here we identify 93 SH2 domains from Legionella that are distinct in sequence and specificity from mammalian SH2 domains. The bacterial SH2 domains are not only capable of binding proteins or peptides in a Tyr phosphorylation-dependent manner, some bind pTyr itself with micromolar affinities, a property not observed for mammalian SH2 domains. The Legionella SH2 domains feature the SH2 fold and a pTyr-binding pocket, but lack a specificity pocket found in a typical mammalian SH2 domain for recognition of sequences flanking the pTyr residue. Our work expands the boundary of phosphotyrosine signalling to prokaryotes, suggesting that some bacterial effector proteins have acquired pTyr-superbinding characteristics to facilitate bacterium-host interactions.

PubMed: 30382091
DOI: 10.1038/s41467-018-06943-2

実験手法

X-RAY DIFFRACTION (1.61 Å)