PDBsum entry 4odl

Isomerase, chaperone

PDB id: 4odl

Contents

Protein chains

150 a.a.

16 a.a.

Ligands

LYS-MET-LYS-PRO-PHE-ILE-PHE-GLY-ALA-NH2

Metals

_CL ×2

Waters ×6

PDB id:

4odl

Name:

Isomerase, chaperone

Title:

Structure of slyd from thermus thermophilus in complex with s2 peptide

Structure:

Peptidyl-prolyl cis-trans isomerase slyd. Chain: a, b. Synonym: ttslyd. Engineered: yes. 30s ribosomal protein s2. Chain: c, d, e, f. Fragment: s2 peptide (unp residues 20-34). Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Gene: ttha0346. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Escherichia coli. Organism_taxid: 83333

Resolution:

2.92Å R-factor: 0.211 R-free: 0.224

Authors:

E.M.Quistgaard,C.Low,P.Nordlund

Key ref:

E.M.Quistgaard et al. (2016). Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD. BMC Biol, 14, 82. PubMed id: 27664121

Date:

10-Jan-14 Release date: 14-Jan-15

Protein chains

Q5SLE7  (Q5SLE7_THET8) -  Peptidyl-prolyl cis-trans isomerase from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 149 a.a.

Struc: 150 a.a.

Protein chains

P0A7V0  (RS2_ECOLI) -  Small ribosomal subunit protein uS2 from Escherichia coli (strain K12)

Seq: 241 a.a.

Struc: 16 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

BMC Biol 14:82 (2016)

PubMed id: 27664121

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.

E.M.Quistgaard, U.Weininger, Y.Ural-Blimke, K.Modig, P.Nordlund, M.Akke, C.Löw.

ABSTRACT

No abstract given.