PDBsum entry 3jvv

Atp binding protein

PDB id: 3jvv

Contents

Protein chains

331 a.a. *

Ligands

ACP ×3

CIT

Metals

_MG ×3

Waters ×89

* Residue conservation analysis

PDB id:

3jvv

Name:

Atp binding protein

Title:

Crystal structure of p. Aeruginosa pilt with bound amp-pcp

Structure:

Twitching mobility protein. Chain: a, b, c. Engineered: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Strain: pa103. Gene: pa0395, pilt. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å R-factor: 0.247 R-free: 0.291

Authors:

A.M.Misic,K.A.Satyshur,K.T.Forest

Key ref:

A.M.Misic et al. (2010). P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor. J Mol Biol, 400, 1011-1021. PubMed id: 20595000

Date:

17-Sep-09 Release date: 02-Jun-10

Protein chains

P24559  (PILT_PSEAE) -  Type IV pilus retractation ATPase PilT from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

Seq: 344 a.a.

Struc: 331 a.a.

J Mol Biol 400:1011-1021 (2010)

PubMed id: 20595000

P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor.

A.M.Misic, K.A.Satyshur, K.T.Forest.

ABSTRACT

Type IV pili are bacterial extracellular filaments that can be retracted to create force and motility. Retraction is accomplished by the motor protein PilT. Crystal structures of Pseudomonas aeruginosa PilT with and without bound beta,gamma-methyleneadenosine-5'-triphosphate have been solved at 2.6 A and 3.1 A resolution, respectively, revealing an interlocking hexamer formed by the action of a crystallographic 2-fold symmetry operator on three subunits in the asymmetric unit and held together by extensive ionic interactions. The roles of two invariant carboxylates, Asp Box motif Glu163 and Walker B motif Glu204, have been assigned to Mg(2+) binding and catalysis, respectively. The nucleotide ligands in each of the subunits in the asymmetric unit of the beta,gamma-methyleneadenosine-5'-triphosphate-bound PilT are not equally well ordered. Similarly, the three subunits in the asymmetric unit of both structures exhibit differing relative conformations of the two domains. The 12 degrees and 20 degrees domain rotations indicate motions that occur during the ATP-coupled mechanism of the disassembly of pili into membrane-localized pilin monomers. Integrating these observations, we propose a three-state "Ready, Active, Release" model for the action of PilT.