PDBsum entry 3wkm

Hydrolase

PDB id: 3wkm

Contents

Protein chains

176 a.a.

216 a.a.

215 a.a.

194 a.a.

Waters ×387

PDB id:

3wkm

Name:

Hydrolase

Title:

The periplasmic pdz tandem fragment of the rsep homologue from aquifex aeolicus in complex with the fab fragment

Structure:

Putative zinc metalloprotease aq_1964. Chain: a, b. Fragment: pdz tandem fragment, unp residues 115-292. Engineered: yes. Mouse igg1-kappa fab (heavy chain). Chain: h, i. Mouse igg1-kappa fab (light chain). Chain: l, m

Source:

Aquifex aeolicus. Organism_taxid: 224324. Strain: vf5. Gene: aq_1964. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. Organism_taxid: 10090. Organism_taxid: 10090

Resolution:

2.20Å R-factor: 0.227 R-free: 0.272

Authors:

T.Nogi,S.Tabata,K.Tamura-Kawakami,J.Takagi

Key ref:

Y.Hizukuri et al. (2014). A structure-based model of substrate discrimination by a noncanonical PDZ tandem in the intramembrane-cleaving protease RseP. Structure, 22, 326-336. PubMed id: 24389025 DOI: 10.1016/j.str.2013.12.003

Date:

28-Oct-13 Release date: 18-Dec-13

Protein chains

O67776  (Y1964_AQUAE) -  Putative zinc metalloprotease aq_1964 from Aquifex aeolicus (strain VF5)

Seq: 429 a.a.

Struc: 176 a.a.

Protein chain

No UniProt id for this chain

Struc: 216 a.a.

Protein chains

No UniProt id for this chain

Struc: 215 a.a.

Protein chain

No UniProt id for this chain

Struc: 194 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.4.24.- - ?????

DOI no: 10.1016/j.str.2013.12.003

Structure 22:326-336 (2014)

PubMed id: 24389025

A structure-based model of substrate discrimination by a noncanonical PDZ tandem in the intramembrane-cleaving protease RseP.

Y.Hizukuri, T.Oda, S.Tabata, K.Tamura-Kawakami, R.Oi, M.Sato, J.Takagi, Y.Akiyama, T.Nogi.

ABSTRACT

During the extracytoplasmic stress response in Escherichia coli, the intramembrane protease RseP cleaves the anti-σ(E) protein RseA only after the membrane-anchored protease DegS truncates the periplasmic part of RseA that suppresses the action of RseP. Here we analyzed the three-dimensional structure of the two tandemly arranged PSD-95/Dlg/ZO-1 (PDZ) domains (PDZ tandem) present in the periplasmic region of RseP and revealed that the two putative ligand-binding grooves constitute a single pocket-like structure that would lie just above the active center sequestrated within the membrane. Complete removal of the PDZ tandem from RseP led to the intramembrane cleavage of RseA without prior truncation by DegS. Furthermore, mutations expected to destabilize the tertiary structure of the PDZ tandem also caused the deregulation of the sequential cleavage. These observations suggest that the PDZ tandem serves as a size-exclusion filter to accommodate the truncated form of RseA into the active center.