PDBsum entry 4tsm

Cell adhesion

PDB id: 4tsm

Contents

Protein chains

505 a.a.

Ligands

GLC-GLC-GLC-GLC ×3

TMO ×19

Waters ×797

PDB id:

4tsm

Name:

Cell adhesion

Title:

Mbp-fusion protein of pila1 from c. Difficile r20291 residues 26-166

Structure:

Maltose-binding protein, pilin chimera. Chain: a, b, c. Fragment: unp residues 27-392 (mbp), unp residues 35-173 (pila1). Synonym: mbp, mmbp,pila1. Engineered: yes

Source:

Escherichia coli, peptoclostridium difficile r20291. Organism_taxid: 562, 645463. Gene: male, hmpref9530_03068, cdr20291_3350. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693

Resolution:

1.90Å R-factor: 0.197 R-free: 0.233

Authors:

K.H.Piepenbrink,E.J.Sundberg

Key ref:

K.H.Piepenbrink et al. (2015). Structural and evolutionary analyses show unique stabilization strategies in the type IV pili of Clostridium difficile. Structure, 23, 385-396. PubMed id: 25599642 DOI: 10.1016/j.str.2014.11.018

Date:

19-Jun-14 Release date: 14-Jan-15

Protein chains

P0AEX9  (MALE_ECOLI) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)

Seq: 396 a.a.

Struc: 505 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2014.11.018

Structure 23:385-396 (2015)

PubMed id: 25599642

Structural and evolutionary analyses show unique stabilization strategies in the type IV pili of Clostridium difficile.

K.H.Piepenbrink, G.A.Maldarelli, C.F.Martinez de la Peña, T.C.Dingle, G.L.Mulvey, A.Lee, E.von Rosenvinge, G.D.Armstrong, M.S.Donnenberg, E.J.Sundberg.

ABSTRACT

Type IV pili are produced by many pathogenic Gram-negative bacteria and are important for processes as diverse as twitching motility, biofilm formation, cellular adhesion, and horizontal gene transfer. However, many Gram-positive species, including Clostridium difficile, also produce type IV pili. Here, we identify the major subunit of the type IV pili of C. difficile, PilA1, and describe multiple 3D structures of PilA1, demonstrating the diversity found in three strains of C. difficile. We also model the incorporation of both PilA1 and a minor pilin, PilJ, into the pilus fiber. Although PilA1 contains no cysteine residues, and therefore cannot form the disulfide bonds found in all Gram-negative type IV pilins, it adopts unique strategies to achieve a typical pilin fold. The structures of PilA1 and PilJ exhibit similarities with the type IVb pilins from Gram-negative bacteria that suggest that the type IV pili of C. difficile are involved in microcolony formation.