PDBsum entry 4nh0

Cell cycle

PDB id: 4nh0

Contents

Protein chains

861 a.a.

Ligands

SO4 ×2

ATP ×4

Metals

_MG ×4

Waters ×8

PDB id:

4nh0

Name:

Cell cycle

Title:

Cytoplasmic domain of the thermomonospora curvata type vii secretion atpase eccc

Structure:

Cell divisionftsk/spoiiie. Chain: a, b. Fragment: cytoplasmic domain of eccc atpase, unp residues 200-1315. Engineered: yes

Source:

Thermomonospora curvata. Organism_taxid: 471852. Strain: atcc 19995 / dsm 43183 / jcm 3096 / ncimb 10081. Gene: tcur_0607. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.90Å R-factor: 0.227 R-free: 0.246

Authors:

O.S.Rosenberg,J.S.Cox,R.M.Stroud,N.Strauli,D.Dovala

Key ref:

O.S.Rosenberg et al. (2015). Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. Cell, 161, 501-512. PubMed id: 25865481 DOI: 10.1016/j.cell.2015.03.040

Date:

03-Nov-13 Release date: 11-Feb-15

Protein chains

D1A4G7  (ECCC_THECD) -  ESX secretion system protein EccC from Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)

Seq: 1315 a.a.

Struc: 861 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.cell.2015.03.040

Cell 161:501-512 (2015)

PubMed id: 25865481

Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion.

O.S.Rosenberg, D.Dovala, X.Li, L.Connolly, A.Bendebury, J.Finer-Moore, J.Holton, Y.Cheng, R.M.Stroud, J.S.Cox.

ABSTRACT

Mycobacterium tuberculosis and Staphylococcus aureus secrete virulence factors via type VII protein secretion (T7S), a system that intriguingly requires all of its secretion substrates for activity. To gain insights into T7S function, we used structural approaches to guide studies of the putative translocase EccC, a unique enzyme with three ATPase domains, and its secretion substrate EsxB. The crystal structure of EccC revealed that the ATPase domains are joined by linker/pocket interactions that modulate its enzymatic activity. EsxB binds via its signal sequence to an empty pocket on the C-terminal ATPase domain, which is accompanied by an increase in ATPase activity. Surprisingly, substrate binding does not activate EccC allosterically but, rather, by stimulating its multimerization. Thus, the EsxB substrate is also an integral T7S component, illuminating a mechanism that helps to explain interdependence of substrates, and suggests a model in which binding of substrates modulates their coordinate release from the bacterium.