PDBsum entry 4htt

Hydrolase

PDB id: 4htt

Contents

Protein chains

225 a.a.

PDB id:

4htt

Name:

Hydrolase

Title:

Crystal structure of twin arginine translocase receptor- tatc in ddm

Structure:

Sec-independent protein translocase protein tatc, lysozyme. Chain: a, b. Synonym: endolysin, lysis protein, muramidase. Engineered: yes

Source:

Aquifex aeolicus vf5, enterobacteria phage t4. Organism_taxid: 224324, 10665. Strain: vf5. Gene: tatc, aq_1267, e. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

6.80Å R-factor: 0.344 R-free: 0.418

Authors:

S.Ramasamy,C.J.M.Suloway,W.M.Clemons Jr.

Key ref:

S.Ramasamy et al. (2013). The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation. Structure, 21, 777-788. PubMed id: 23583035 DOI: 10.1016/j.str.2013.03.004

Date:

01-Nov-12 Release date: 01-May-13

Protein chains

O67305  (TATC_AQUAE) -  Sec-independent protein translocase protein TatC from Aquifex aeolicus (strain VF5)

Seq: 240 a.a.

Struc: 225 a.a.

Protein chains

P00720  (ENLYS_BPT4) -  Endolysin from Enterobacteria phage T4

Seq: 164 a.a.

Struc: 225 a.a.*

* PDB and UniProt seqs differ at 143 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1016/j.str.2013.03.004

Structure 21:777-788 (2013)

PubMed id: 23583035

The glove-like structure of the conserved membrane protein TatC provides insight into signal sequence recognition in twin-arginine translocation.

S.Ramasamy, R.Abrol, C.J.Suloway, W.M.Clemons.

ABSTRACT

In bacteria, two signal-sequence-dependent secretion pathways translocate proteins across the cytoplasmic membrane. Although the mechanism of the ubiquitous general secretory pathway is becoming well understood, that of the twin-arginine translocation pathway, responsible for translocation of folded proteins across the bilayer, is more mysterious. TatC, the largest and most conserved of three integral membrane components, provides the initial binding site of the signal sequence prior to pore assembly. Here, we present two crystal structures of TatC from the thermophilic bacteria Aquifex aeolicus at 4.0 Å and 6.8 Å resolution. The membrane architecture of TatC includes a glove-shaped structure with a lipid-exposed pocket predicted by molecular dynamics to distort the membrane. Correlating the biochemical literature to these results suggests that the signal sequence binds in this pocket, leading to structural changes that facilitate higher order assemblies.