PDBsum entry 5l3w

Protein transport

PDB id: 5l3w

Contents

Protein chain

297 a.a.

Ligands

GDP

SO4

Waters ×40

PDB id:

5l3w

Name:

Protein transport

Title:

Structure of the crenarchaeal ftsy gtpase bound to gdp

Structure:

Signal recognition particle receptor ftsy. Chain: a. Fragment: ng domain, unp residues 69-368. Synonym: srp receptor. Engineered: yes

Source:

Sulfolobus acidocaldarius. Organism_taxid: 2285. Gene: ftsy, aty89_10730, atz20_02285. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.176 R-free: 0.218

Authors:

G.Bange,K.Wild,I.Sinning

Key ref:

K.Wild et al. (2016). Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex. J Mol Biol, 428, 2880-2897. PubMed id: 27241309 DOI: 10.1016/j.jmb.2016.05.015

Date:

24-May-16 Release date: 08-Jun-16

Protein chain

P27414  (FTSY_SULAC) -  Signal recognition particle receptor FtsY from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

Seq: 369 a.a.

Struc: 297 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.5.4 - signal-recognition-particle GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP + H2O = GDP (Bound ligand (Het Group name = GDP) corresponds exactly) + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.jmb.2016.05.015

J Mol Biol 428:2880-2897 (2016)

PubMed id: 27241309

Structural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex.

K.Wild, G.Bange, D.Motiejunas, J.Kribelbauer, A.Hendricks, B.Segnitz, R.C.Wade, I.Sinning.

ABSTRACT

The signal recognition particle (SRP) is a ribonucleoprotein complex with a key role in targeting and insertion of membrane proteins. The two SRP GTPases, SRP54 (Ffh in bacteria) and FtsY (SRα in eukaryotes), form the core of the targeting complex (TC) regulating the SRP cycle. The architecture of the TC and its stimulation by RNA has been described for the bacterial SRP system while this information is lacking for other domains of life. Here, we present the crystal structures of the GTPase heterodimers of archaeal (Sulfolobus solfataricus), eukaryotic (Homo sapiens), and chloroplast (Arabidopsis thaliana) SRP systems. The comprehensive structural comparison combined with Brownian dynamics simulations of TC formation allows for the description of the general blueprint and of specific adaptations of the quasi-symmetric heterodimer. Our work defines conserved external nucleotide-binding sites for SRP GTPase activation by RNA. Structural analyses of the GDP-bound, post-hydrolysis states reveal a conserved, magnesium-sensitive switch within the I-box. Overall, we provide a general model for SRP cycle regulation by RNA.