PDBsum entry 2nd9

Cell cycle

PDB id: 2nd9

Contents

Protein chain

135 a.a.

PDB id:

2nd9

Name:

Cell cycle

Title:

Solution structure of mapz extracellular domain first subdomain

Structure:

Mid-cell-anchored protein z. Chain: a. Fragment: first subdomain (q178 - g313) of mapz extracellular domain. Engineered: yes

Source:

Streptococcus pneumoniae r6. Streptococcus pneumoniae. Organism_taxid: 171101. Strain: r6. Gene: mapz, spr0334. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

N.L.Jean,S.Manuse,M.Guinot,C.M.Bougault,C.Grangeasse,J.-P.Simorre

Key ref:

S.Manuse et al. (2016). Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. Nat Commun, 7, 12071. PubMed id: 27346279

Date:

11-May-16 Release date: 29-Jun-16

Protein chain

Q8DR55  (MAPZ_STRR6) -  Mid-cell-anchored protein Z from Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

Seq: 464 a.a.

Struc: 135 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

Nat Commun 7:12071 (2016)

PubMed id: 27346279

Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ.

S.Manuse, N.L.Jean, M.Guinot, J.P.Lavergne, C.Laguri, C.M.Bougault, M.S.VanNieuwenhze, C.Grangeasse, J.P.Simorre.

ABSTRACT

Accurate placement of the bacterial division site is a prerequisite for the generation of two viable and identical daughter cells. In Streptococcus pneumoniae, the positive regulatory mechanism involving the membrane protein MapZ positions precisely the conserved cell division protein FtsZ at the cell centre. Here we characterize the structure of the extracellular domain of MapZ and show that it displays a bi-modular structure composed of two subdomains separated by a flexible serine-rich linker. We further demonstrate in vivo that the N-terminal subdomain serves as a pedestal for the C-terminal subdomain, which determines the ability of MapZ to mark the division site. The C-terminal subdomain displays a patch of conserved amino acids and we show that this patch defines a structural motif crucial for MapZ function. Altogether, this structure-function analysis of MapZ provides the first molecular characterization of a positive regulatory process of bacterial cell division.