PDBsum entry 6e8h

Peptide binding protein

PDB id: 6e8h

Contents

Protein chain

158 a.a.

Metals

_CL

Waters ×243

PDB id:

6e8h

Name:

Peptide binding protein

Title:

Legionella longbeachae lesh (llo2327)

Structure:

Lesh (llo2327). Chain: a. Engineered: yes

Source:

Legionella longbeachae serogroup 1 (strain nsw150). Organism_taxid: 661367. Strain: nsw150. Gene: llo_2327. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.68Å R-factor: 0.214 R-free: 0.248

Authors:

T.Kaneko,S.S.C.Li

Key ref:

T.Kaneko et al. (2018). Identification and characterization of a large family of superbinding bacterial SH2 domains. Nat Commun, 9, 4549. PubMed id: 30382091

Date:

29-Jul-18 Release date: 14-Nov-18

Protein chain

D3HJY4  (D3HJY4_LEGLN) -  SH2 domain-containing protein from Legionella longbeachae serogroup 1 (strain NSW150)

Seq: 167 a.a.

Struc: 158 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Nat Commun 9:4549 (2018)

PubMed id: 30382091

Identification and characterization of a large family of superbinding bacterial SH2 domains.

T.Kaneko, P.J.Stogios, X.Ruan, C.Voss, E.Evdokimova, T.Skarina, A.Chung, X.Liu, L.Li, A.Savchenko, A.W.Ensminger, S.S.Li.

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.