PDBsum entry 4ppd

Structural protein

PDB id: 4ppd

Contents

Protein chains

92 a.a.

82 a.a.

87 a.a.

Ligands

SO4 ×7

GOL ×2

Waters ×62

PDB id:

4ppd

Name:

Structural protein

Title:

Pdua k26a, crystal form 2

Structure:

Propanediol utilization protein pdua. Chain: a, b, c, d, e, f, g. Engineered: yes. Mutation: yes

Source:

Salmonella enterica subsp. Enterica serovar typhimurium. Organism_taxid: 99287. Strain: lt2 / sgsc1412 / atcc 700720. Gene: pdua, stm2038. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.40Å R-factor: 0.197 R-free: 0.219

Authors:

D.E.Mcnamara,M.R.Sawaya,T.A.Bobik,T.O.Yeates

Key ref:

S.Sinha et al. (2014). Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J Mol Biol, 426, 2328-2345. PubMed id: 24747050 DOI: 10.1016/j.jmb.2014.04.012

Date:

26-Feb-14 Release date: 14-May-14

Protein chains

P0A1C7  (PDUA_SALTY) -  Bacterial microcompartment shell protein PduA from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 94 a.a.

Struc: 92 a.a.*

Protein chain

P0A1C7  (PDUA_SALTY) -  Bacterial microcompartment shell protein PduA from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 94 a.a.

Struc: 82 a.a.*

Protein chains

P0A1C7  (PDUA_SALTY) -  Bacterial microcompartment shell protein PduA from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

Seq: 94 a.a.

Struc: 87 a.a.*

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

DOI no: 10.1016/j.jmb.2014.04.012

J Mol Biol 426:2328-2345 (2014)

PubMed id: 24747050

Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment.

S.Sinha, S.Cheng, Y.W.Sung, D.E.McNamara, M.R.Sawaya, T.O.Yeates, T.A.Bobik.

ABSTRACT

Bacterial microcompartments (MCPs) are the simplest organelles known. They function to enhance metabolic pathways by confining several related enzymes inside an all-protein envelope called the shell. In this study, we investigated the factors that govern MCP assembly by performing scanning mutagenesis on the surface residues of PduA, a major shell protein of the MCP used for 1,2-propanediol degradation. Biochemical, genetic, and structural analysis of 20 mutants allowed us to determine that PduA K26, N29, and R79 are crucial residues that stabilize the shell of the 1,2-propanediol MCP. In addition, we identify two PduA mutants (K37A and K55A) that impair MCP function most likely by altering the permeability of its protein shell. These are the first studies to examine the phenotypic effects of shell protein structural mutations in an MCP system. The findings reported here may be applicable to engineering protein containers with improved stability for biotechnology applications.