4ODO

Structure of SlyD from Thermus thermophilus in complex with FK506

Summary for 4ODO

• Entry DOI: 10.2210/pdb4odo/pdb
• Related: 4ODK 4ODL 4ODM 4ODN 4ODP 4ODQ 4ODR
• Descriptor: Peptidyl-prolyl cis-trans isomerase SlyD, MAGNESIUM ION, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: fkbp domain, if domain, chaperone, peptidyl-prolyl isomerase, ppiase, isomerase
• Biological source: Thermus thermophilus (human)
• Total number of polymer chains: 3
• Total formula weight: 55117.67

Authors

Quistgaard, E.M.,Low, C.,Nordlund, P. (deposition date: 2014-01-10, release date: 2015-01-14, Last modification date: 2024-02-28)

Primary citation

Quistgaard, E.M.,Weininger, U.,Ural-Blimke, Y.,Modig, K.,Nordlund, P.,Akke, M.,Low, C.
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
BMC Biol., 14:82-82, 2016

PubMed Abstract: Peptidyl-prolyl isomerases (PPIases) catalyze cis/trans isomerization of peptidyl-prolyl bonds, which is often rate-limiting for protein folding. SlyD is a two-domain enzyme containing both a PPIase FK506-binding protein (FKBP) domain and an insert-in-flap (IF) chaperone domain. To date, the interactions of these domains with unfolded proteins have remained rather obscure, with structural information on binding to the FKBP domain being limited to complexes involving various inhibitor compounds or a chemically modified tetrapeptide.

PubMed: 27664121
DOI: 10.1186/s12915-016-0300-3

Experimental method

X-RAY DIFFRACTION (1.599 Å)