 |
PDBsum entry 4c7o
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Nuclear protein/RNA
|
PDB id
|
|
|
|
4c7o
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
The structural basis of ftsy recruitment and gtpase activation by srp RNA.
|
 |
|
Authors
|
 |
F.Voigts-Hoffmann,
N.Schmitz,
K.Shen,
S.O.Shan,
S.F.Ataide,
N.Ban.
|
 |
|
Ref.
|
 |
Mol Cell, 2013,
52,
643-654.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The universally conserved signal recognition particle (SRP) system mediates the
targeting of membrane proteins to the translocon in a multistep process
controlled by GTP hydrolysis. Here we present the 2.6 Å crystal structure of
the GTPase domains of the E. coli SRP protein (Ffh) and its receptor (FtsY) in
complex with the tetraloop and the distal region of SRP-RNA, trapped in the
activated state in presence of GDP:AlF4. The structure reveals the atomic
details of FtsY recruitment and, together with biochemical experiments,
pinpoints G83 as the key RNA residue that stimulates GTP hydrolysis. Insertion
of G83 into the FtsY active site orients a single glutamate residue provided by
Ffh (E277), triggering GTP hydrolysis and complex disassembly at the end of the
targeting cycle. The complete conservation of the key residues of the SRP-RNA
and the SRP protein implies that the suggested chemical mechanism of GTPase
activation is applicable across all kingdoms.
|
 |
|
|
|
|
 |