PDBsum entry 5ebd

Protein transport

PDB id: 5ebd

Contents

Protein chain

379 a.a.

Metals

_CL ×2

_CA

Waters ×46

PDB id:

5ebd

Name:

Protein transport

Title:

Crystal structure of eccb1 of mycobacterium tuberculosis in spacegroup p21 (state iv)

Structure:

Esx-1 secretion system protein eccb1. Chain: a. Fragment: unp residues 72-480. Synonym: esx conserved component b1,type vii secretion system protein eccb1,t7ss protein eccb1. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: atcc 25618 / h37rv. Gene: eccb1, rv3869. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.60Å R-factor: 0.226 R-free: 0.283

Authors:

X.L.Zhang,C.Qi,X.Q.Xie,D.F.Li,L.J.Bi

Key ref:

X.Q.Xie et al. (2016). Crystallographic observation of the movement of the membrane-distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis. Acta Crystallogr F Struct Biol Commun, 72, 139-144. PubMed id: 26841765 DOI: 10.1107/S2053230X16000212

Date:

19-Oct-15 Release date: 17-Feb-16

Protein chain

P9WNR7  (ECCB1_MYCTU) -  ESX-1 secretion system ATPase EccB1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 480 a.a.

Struc: 379 a.a.

Enzyme reactions

• Enzyme class: E.C.3.6.-.-

DOI no: 10.1107/S2053230X16000212

Acta Crystallogr F Struct Biol Commun 72:139-144 (2016)

PubMed id: 26841765

Crystallographic observation of the movement of the membrane-distal domain of the T7SS core component EccB1 from Mycobacterium tuberculosis.

X.Q.Xie, X.L.Zhang, C.Qi, D.F.Li, J.Fleming, D.C.Wang, L.J.Bi.

ABSTRACT

The protein EccB1, a core component of the type VII secretion system (T7SS) of Mycobacterium tuberculosis, has been identified as an ATPase and is essential for the secretion of virulence factors by the ESX-1 system. In a previous study, EccB1 structures were determined in two different conformations. Here, two new conformations are identified and described. These four conformations present snapshots of the swinging movement of the membrane-distal domain A2. The movement of this domain involves conformational changes in two flexible loops (loop A, residues 243-264, and loop B, residues 324-341) which are rich in proline and glycine residues and connect domain A2 to domains C1 and B2. It is proposed that the movement of this domain is related to the ATPase activity of EccB1 and its homologues, as well as to the substrate transport of ESX secretion systems.