3JVU

Crystal structure of unliganded P. aeruginosa PilT

3JVU の概要

• エントリーDOI: 10.2210/pdb3jvu/pdb
• 関連するPDBエントリー: 2EWV 2EWW 2GSZ 3JVV
• 分子名称: Twitching mobility protein, CHLORIDE ION, CITRIC ACID, ... (4 entities in total)
• 機能のキーワード: motor protein, p-loop atpase, type iv pili, atp-binding, fimbrium, nucleotide-binding, transport, atp binding protein
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Cytoplasm (Probable): P24559
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 118506.01

構造登録者

Misic, A.M.,Satyshur, K.A.,Forest, K.T. (登録日: 2009-09-17, 公開日: 2010-07-21, 最終更新日: 2023-09-06)

主引用文献

Misic, A.M.,Satyshur, K.A.,Forest, K.T.
P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor.
J.Mol.Biol., 400:1011-1021, 2010

PubMed 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.

PubMed: 20595000
DOI: 10.1016/j.jmb.2010.05.066

実験手法

X-RAY DIFFRACTION (3.1 Å)