PDBsum entry 4zlh

Metal binding protein

PDB id: 4zlh

Contents

Protein chains

323 a.a.

Metals

_ZN ×2

Waters ×295

PDB id:

4zlh

Name:

Metal binding protein

Title:

Structure of the lapb cytoplasmic domain at 2 angstroms

Structure:

Lipopolysaccharide assembly protein b. Chain: a, b. Fragment: unp residues 51-389. Engineered: yes

Source:

Escherichia coli o157:h7. Organism_taxid: 83334. Gene: lapb, ycim, z2526, ecs1853. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.00Å R-factor: 0.206 R-free: 0.255

Authors:

C.C.Prince,Z.Jia

Key ref:

C.Prince and Z.Jia (2015). An Unexpected Duo: Rubredoxin Binds Nine TPR Motifs to Form LapB, an Essential Regulator of Lipopolysaccharide Synthesis. Structure, 23, 1500-1506. PubMed id: 26190574 DOI: 10.1016/j.str.2015.06.011

Date:

01-May-15 Release date: 11-Nov-15

Protein chains

P0AB60  (LAPB_ECO57) -  Lipopolysaccharide assembly protein B from Escherichia coli O157:H7

Seq: 389 a.a.

Struc: 323 a.a.

DOI no: 10.1016/j.str.2015.06.011

Structure 23:1500-1506 (2015)

PubMed id: 26190574

An Unexpected Duo: Rubredoxin Binds Nine TPR Motifs to Form LapB, an Essential Regulator of Lipopolysaccharide Synthesis.

C.Prince, Z.Jia.

ABSTRACT

Lipopolysaccharide (LPS) synthesis and export are essential pathways for bacterial growth, proliferation, and virulence. The essential protein LapB from Escherichia coli has recently been identified as a regulator of LPS synthesis. We have determined the crystal structure of LapB (without the N-terminal transmembrane helix) at 2 Å resolution using zinc single-wavelength anomalous diffraction phasing derived from a single bound zinc atom. This structure demonstrates the presence of nine tetratricopeptide repeats (TPR) motifs, including two TPR folds that were not predicted from sequence, and a rubredoxin-type metal binding domain. The rubredoxin domain is bound intimately to the TPR motifs, which has not been previously observed or predicted. Mutations in the rubredoxin/TPR interface inhibit in vivo cell growth, and in vitro studies indicate that these modifications cause local displacement of rubredoxin from its binding site without changing the secondary structure of LapB. LapB is the first reported structure to contain both a rubredoxin domain and TPR motifs.