First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

3cgn

From Proteopedia

Jump to: navigation, search


3cgn, resolution 2.70Å ()
Ligands:
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Related: 3cgm
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of thermophilic SlyD

Publication Abstract from PubMed

SlyD (sensitive to lysis D; product of the slyD gene) is a prolyl isomerase [peptidyl-prolyl cis/trans isomerase (PPIase)] of the FK506 binding protein (FKBP) type with chaperone properties. X-ray structures derived from three different crystal forms reveal that SlyD from Thermus thermophilus consists of two domains representing two functional units. PPIase activity is located in a typical FKBP domain, whereas chaperone function is associated with the autonomously folded insert-in-flap (IF) domain. The two isolated domains are stable and functional in solution, but the presence of the IF domain increases the PPIase catalytic efficiency of the FKBP domain by 2 orders of magnitude, suggesting that the two domains act synergistically to assist the folding of polypeptide chains. The substrate binding surface of SlyD from T. thermophilus was mapped by NMR chemical shift perturbations to hydrophobic residues of the IF domain, which exhibits significantly reduced thermodynamic stability according to NMR hydrogen/deuterium exchange and fluorescence equilibrium transition experiments. Based on structural homologies, we hypothesize that this is due to the absence of a stabilizing beta-strand, suggesting in turn a mechanism for chaperone activity by 'donor-strand complementation.' Furthermore, we identified a conserved metal (Ni(2+)) binding site at the C-terminal SlyD-specific helical appendix of the FKBP domain, which may play a role in metalloprotein assembly.

Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus., Low C, Neumann P, Tidow H, Weininger U, Haupt C, Friedrich-Epler B, Scholz C, Stubbs MT, Balbach J, J Mol Biol. 2010 May 7;398(3):375-90. Epub 2010 Mar 15. PMID:20230833

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3cgn is a 1 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

  • Low C, Neumann P, Tidow H, Weininger U, Haupt C, Friedrich-Epler B, Scholz C, Stubbs MT, Balbach J. Crystal structure determination and functional characterization of the metallochaperone SlyD from Thermus thermophilus. J Mol Biol. 2010 May 7;398(3):375-90. Epub 2010 Mar 15. PMID:20230833 doi:10.1016/j.jmb.2010.03.014

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools