 |
PDBsum entry 6e8h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Peptide binding protein
|
PDB id
|
|
|
|
6e8h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Identification and characterization of a large family of superbinding bacterial sh2 domains.
|
|
|
Authors
|
|
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.
|
|
|
Ref.
|
|
Nat Commun, 2018,
9,
4549.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
