PDBsum entry 4l1c

Protein binding

PDB id: 4l1c

Contents

Protein chains

98 a.a.

Waters ×19

PDB id:

4l1c

Name:

Protein binding

Title:

Crystal structure of dimerized n-terminal domain of minc

Structure:

Probable septum site-determining protein minc. Chain: a, b. Fragment: unp residues 8-105. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 364106. Strain: uti89 / upec. Gene: ecdh1me8569_1115, ecdh1_2472, minc, uti89_c1361. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.28Å R-factor: 0.229 R-free: 0.263

Authors:

J.Y.An,T.G.Kim,K.R.Park,J.G.Lee,H.S.Youn,J.Y.Kang,Y.Lee,G.B.Kang, S.H.Eom

Key ref:

J.Y.An et al. (2013). Crystal structure of the N-terminal domain of MinC dimerized via domain swapping. J Synchrotron Radiat, 20, 984-988. PubMed id: 24121353 DOI: 10.1107/S0909049513022760

Date:

03-Jun-13 Release date: 23-Oct-13

Protein chains

Q1RCS1  (Q1RCS1_ECOUT) -  Probable septum site-determining protein MinC from Escherichia coli (strain UTI89 / UPEC)

Seq: 236 a.a.

Struc: 98 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1107/S0909049513022760

J Synchrotron Radiat 20:984-988 (2013)

PubMed id: 24121353

Crystal structure of the N-terminal domain of MinC dimerized via domain swapping.

J.Y.An, T.G.Kim, K.R.Park, J.G.Lee, H.S.Youn, Y.Lee, J.Y.Kang, G.B.Kang, S.H.Eom.

ABSTRACT

Proper cell division at the mid-site of gram-negative bacteria reflects critical regulation by the min system (MinC, MinD and MinE) of the cytokinetic Z ring, which is a polymer composed of FtsZ subunits. MinC and MinD act together to inhibit aberrantly positioned Z-ring formation. MinC consists of two domains: an N-terminal domain (MinCNTD), which interacts with FtsZ and inhibits FtsZ polymerization, and a C-terminal domain (MinCCTD), which interacts with MinD and inhibits the bundling of FtsZ filaments. These two domains reportedly function together, and both are essential for normal cell division. The full-length dimeric structure of MinC from Thermotoga maritima has been reported, and shows that MinC dimerization occurs via MinCCTD; MinCNTD is not involved in dimerization. Here the crystal structure of Escherichia coli MinCNTD (EcoMinCNTD) is reported. EcoMinCNTD forms a dimer via domain swapping between the first β strands in each subunit. It is therefore suggested that the dimerization of full-length EcoMinC occurs via both MinCCTD and MinCNTD, and that the dimerized EcoMinCNTD likely plays an important role in inhibiting aberrant Z-ring localization.