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Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site

DOI: 10.1016/j.fob.2015.03.013 DOI Help
PMID: 25905034 PMID Help

Authors: Shalini Iyer (University of Bath) , Penelope J. La-borde (University of Bath) , Karl A. P. Payne (University of Manchester) , Mark R. Parsons (University of Leeds) , Anthony J. Turner (University of Leeds) , R. Elwyn Isaac (University of Leeds) , K. Ravi Acharya (University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Open Bio , VOL 5 , PAGES 292 - 302

State: Published (Approved)
Published: April 2015
Diamond Proposal Number(s): 8922

Open Access Open Access

Abstract: Eukaryotic aminopeptidase P1 (APP1), also known as X-prolyl aminopeptidase (XPNPEP1) in human tissues, is a cytosolic exopeptidase that preferentially removes amino acids from the N-terminus of peptides possessing a penultimate N-terminal proline residue. The enzyme has an important role in the catabolism of proline containing peptides since peptide bonds adjacent to the imino acid proline are resistant to cleavage by most peptidases. We show that recombinant and catalytically active Caenorhabditis elegans APP-1 is a dimer that uses dinuclear zinc at the active site and, for the first time, we provide structural information for a eukaryotic APP-1 in complex with the inhibitor, apstatin. Our analysis reveals that C. elegans APP-1 shares similar mode of substrate binding and a common catalytic mechanism with other known X-prolyl aminopeptidases

Journal Keywords: Apstatin; Di-Nuclear Active Site; Protease Inhibitor; X-Ray Crystallography; X-Prolyl Aminopeptidase; Zinc Metalloprotease

Subject Areas: Biology and Bio-materials


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I24-Microfocus Macromolecular Crystallography

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