PDBsum entry 5fv0

Secretion

PDB id: 5fv0

Contents

Protein chains

508 a.a.

458 a.a.

Ligands

ONA

1PE

ATP

Waters ×51

PDB id:

5fv0

Name:

Secretion

Title:

The cytoplasmic domain of essc

Structure:

Esx secretion system protein eccc. Chain: a, b. Fragment: c-terminal fragment, residues 966-1479. Synonym: type vii secretion system protein eccc,t7ss protein eccc. Engineered: yes

Source:

Geobacillus thermodenitrificans. Organism_taxid: 33940. Gene: eccc, essc, gtng_0419. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: plyss

Resolution:

2.91Å R-factor: 0.262 R-free: 0.275

Authors:

M.Zoltner,W.M.A.V.Ng,T.Palmer,W.N.Hunter

Key ref:

M.Zoltner et al. (2016). EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system. Biochem J, 473, 1941-1952. PubMed id: 27130157 DOI: 10.1042/BCJ20160257

Date:

01-Feb-16 Release date: 02-Mar-16

Protein chain

A4IKE7  (ECCC_GEOTN) -  ESX secretion system protein EccC from Geobacillus thermodenitrificans (strain NG80-2)

Seq: 1479 a.a.

Struc: 508 a.a.

Protein chain

A4IKE7  (ECCC_GEOTN) -  ESX secretion system protein EccC from Geobacillus thermodenitrificans (strain NG80-2)

Seq: 1479 a.a.

Struc: 458 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1042/BCJ20160257

Biochem J 473:1941-1952 (2016)

PubMed id: 27130157

EssC: domain structures inform on the elusive translocation channel in the Type VII secretion system.

M.Zoltner, W.M.Ng, J.J.Money, P.K.Fyfe, H.Kneuper, T.Palmer, W.N.Hunter.

ABSTRACT

The membrane-bound protein EssC is an integral component of the bacterial Type VII secretion system (T7SS), which is a determinant of virulence in important Gram-positive pathogens. The protein is predicted to consist of an intracellular repeat of forkhead-associated (FHA) domains at the N-terminus, two transmembrane helices and three P-loop-containing ATPase-type domains, D1-D3, forming the C-terminal intracellular segment. We present crystal structures of the N-terminal FHA domains (EssC-N) and a C-terminal fragment EssC-C from Geobacillus thermodenitrificans, encompassing two of the ATPase-type modules, D2 and D3. Module D2 binds ATP with high affinity whereas D3 does not. The EssC-N and EssC-C constructs are monomeric in solution, but the full-length recombinant protein, with a molecular mass of approximately 169 kDa, forms a multimer of approximately 1 MDa. The observation of protomer contacts in the crystal structure of EssC-C together with similarity to the DNA translocase FtsK, suggests a model for a hexameric EssC assembly. Such an observation potentially identifies the key, and to date elusive, component of pore formation required for secretion by this recently discovered secretion system. The juxtaposition of the FHA domains suggests potential for interacting with other components of the secretion system. The structural data were used to guide an analysis of which domains are required for the T7SS machine to function in pathogenic Staphylococcus aureus The extreme C-terminal ATPase domain appears to be essential for EssC activity as a key part of the T7SS, whereas D2 and FHA domains are required for the production of a stable and functional protein.