PDBsum entry 5c21

Protein transport

PDB id: 5c21

Contents

Protein chains

267 a.a.

PDB id:

5c21

Name:

Protein transport

Title:

Crystal structure of native hlyd from e. Coli

Structure:

Chromosomal hemolysin d. Chain: a, b. Fragment: unp residues 57-333. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: hlyd. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.50Å R-factor: 0.237 R-free: 0.274

Authors:

N.C.Ha,J.S.Kim,B.Y.Yoon

Key ref:

J.S.Kim et al. (2016). Crystal Structure of a Soluble Fragment of the Membrane Fusion Protein HlyD in a Type I Secretion System of Gram-Negative Bacteria. Structure, 24, 477-485. PubMed id: 26833388 DOI: 10.1016/j.str.2015.12.012

Date:

15-Jun-15 Release date: 17-Feb-16

Protein chains

P09986  (HLYDC_ECOLX) -  Hemolysin secretion protein D, chromosomal from Escherichia coli

Seq: 478 a.a.

Struc: 267 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1016/j.str.2015.12.012

Structure 24:477-485 (2016)

PubMed id: 26833388

Crystal Structure of a Soluble Fragment of the Membrane Fusion Protein HlyD in a Type I Secretion System of Gram-Negative Bacteria.

J.S.Kim, S.Song, M.Lee, S.Lee, K.Lee, N.C.Ha.

ABSTRACT

The protein toxin HlyA of Escherichia coli is exported without a periplasmic intermediate by the type I secretion system (T1SS). The T1SS is composed of an inner membrane ABC transporter HlyB, an outer-membrane channel protein TolC, and a membrane fusion protein HlyD. However, the assembly of the T1SS remains to be elucidated. In this study, we determine the crystal structure of a part of the C-terminal periplasmic domain of HlyD. The long α-helical domain consisting of three α helices and a lipoyl domain was identified in the crystal structure. Based on the HlyD structure, we modeled the hexameric assembly of HlyD with a long α-helical barrel, which formed a complex with TolC in an intermeshing cogwheel-to-cogwheel manner, as observed in tripartite RND-type drug efflux pumps. These observations provide a structural blueprint for understanding the type I secretion system in pathogenic Gram-negative bacteria.