5EX1

Crystal structure of cyclophilin AquaCyp300 from Hirschia baltica

Summary for 5EX1

• Entry DOI: 10.2210/pdb5ex1/pdb
• Descriptor: Peptidyl-prolyl cis-trans isomerase cyclophilin type, MAGNESIUM ION (3 entities in total)
• Functional Keywords: cyclophilin, ppiase, rotamase, folding helper, isomerase
• Biological source: Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418)
• Total number of polymer chains: 6
• Total formula weight: 191616.74

Authors

Jakob, R.P.,Maier, T. (deposition date: 2015-11-23, release date: 2016-06-22, Last modification date: 2024-11-06)

Primary citation

Jakob, R.P.,Schmidpeter, P.A.,Koch, J.R.,Schmid, F.X.,Maier, T.
Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.
Plos One, 11:e0157070-e0157070, 2016

PubMed Abstract: Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric species. In addition to a canonical PPIase domain, AquaCyps contain large extensions and insertions. The crystal structures of two representatives from Hirschia baltica, AquaCyp293 and AquaCyp300, reveal the formation of a compact domain, the NIC domain, by the N- and C-terminal extensions together with a central insertion. The NIC domain adopts a novel mixed alpha-helical, beta-sheet fold that is linked to the cyclophilin domain via a conserved disulfide bond. In its overall fold, AquaCyp293 resembles AquaCyp300, but the two proteins utilize distinct sets of active site residues, consistent with differences in their PPIase catalytic properties. While AquaCyp293 is a highly active general PPIase, AquaCyp300 is specific for hydrophobic substrate peptides and exhibits lower overall activity.

PubMed: 27276069
DOI: 10.1371/journal.pone.0157070

Experimental method

X-RAY DIFFRACTION (2.053 Å)