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Title: Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex

Abstract

The glutaminyl cyclase isolated from C. papaya latex has been crystallized using the hanging-drop method. Diffraction data have been collected at ESRF beamline BM14 and processed to 1.7 Å resolution. In living systems, the intramolecular cyclization of N-terminal glutamine residues is accomplished by glutaminyl cyclase enzymes (EC 2.3.2.5). While in mammals these enzymes are involved in the synthesis of hormonal and neurotransmitter peptides, the physiological role played by the corresponding plant enzymes still remains to be unravelled. Papaya glutaminyl cyclase (PQC), a 33 kDa enzyme found in the latex of the tropical tree Carica papaya, displays an exceptional resistance to chemical and thermal denaturation as well as to proteolysis. In order to elucidate its enzymatic mechanism and to gain insights into the structural determinants underlying its remarkable stability, PQC was isolated from papaya latex, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 62.82, b = 81.23, c = 108.17 Å and two molecules per asymmetric unit. Diffraction data have been collected at ESRF beamline BM14 and processed to a resolution of 1.7 Å.

Authors:
 [1]; ;  [2];  [3];  [1];  [4];  [2];  [4];  [5]
  1. Laboratoire de Chimie Générale I, Faculté de Médecine-ULB CP609, 808 Route de Lennik, B-1070 Brussels (Belgium)
  2. CNRS-UMR 8525, Institut de Biologie de Lille, BP 477, 1 Rue du Professeur Calmette, F-59021 Lille (France)
  3. EMBL Grenoble Outstation, 6 Rue Jules Horowitz, BP 181, F-38042 Grenoble CEDEX 9 (France)
  4. Laboratoire de Chimie Générale, Institut de Pharmacie-ULB CP206/04, Boulevard du Triomphe, B-1050 Brussels (Belgium)
  5. (Belgium)
Publication Date:
OSTI Identifier:
22356079
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 61; Journal Issue: Pt 1; Other Information: PMCID: PMC1952388; PMID: 16508091; PUBLISHER-ID: bw5065; OAI: oai:pubmedcentral.nih.gov:1952388; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; EUROPEAN SYNCHROTRON RADIATION FACILITY; LATEX; MOLECULES; RESOLUTION; SPACE GROUPS; STABILITY; SYNTHESIS; X-RAY DIFFRACTION

Citation Formats

Azarkan, Mohamed, Clantin, Bernard, Bompard, Coralie, Belrhali, Hassan, Baeyens-Volant, Danielle, Looze, Yvan, Villeret, Vincent, E-mail: vincent.villeret@ibl.fr, Wintjens, René, E-mail: vincent.villeret@ibl.fr, and Laboratoire de Chimie Générale I, Faculté de Médecine-ULB CP609, 808 Route de Lennik, B-1070 Brussels. Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex. United Kingdom: N. p., 2005. Web. doi:10.1107/S1744309104025904.
Azarkan, Mohamed, Clantin, Bernard, Bompard, Coralie, Belrhali, Hassan, Baeyens-Volant, Danielle, Looze, Yvan, Villeret, Vincent, E-mail: vincent.villeret@ibl.fr, Wintjens, René, E-mail: vincent.villeret@ibl.fr, & Laboratoire de Chimie Générale I, Faculté de Médecine-ULB CP609, 808 Route de Lennik, B-1070 Brussels. Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex. United Kingdom. doi:10.1107/S1744309104025904.
Azarkan, Mohamed, Clantin, Bernard, Bompard, Coralie, Belrhali, Hassan, Baeyens-Volant, Danielle, Looze, Yvan, Villeret, Vincent, E-mail: vincent.villeret@ibl.fr, Wintjens, René, E-mail: vincent.villeret@ibl.fr, and Laboratoire de Chimie Générale I, Faculté de Médecine-ULB CP609, 808 Route de Lennik, B-1070 Brussels. Sat . "Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex". United Kingdom. doi:10.1107/S1744309104025904.
@article{osti_22356079,
title = {Crystallization and preliminary X-ray diffraction studies of the glutaminyl cyclase from Carica papaya latex},
author = {Azarkan, Mohamed and Clantin, Bernard and Bompard, Coralie and Belrhali, Hassan and Baeyens-Volant, Danielle and Looze, Yvan and Villeret, Vincent, E-mail: vincent.villeret@ibl.fr and Wintjens, René, E-mail: vincent.villeret@ibl.fr and Laboratoire de Chimie Générale I, Faculté de Médecine-ULB CP609, 808 Route de Lennik, B-1070 Brussels},
abstractNote = {The glutaminyl cyclase isolated from C. papaya latex has been crystallized using the hanging-drop method. Diffraction data have been collected at ESRF beamline BM14 and processed to 1.7 Å resolution. In living systems, the intramolecular cyclization of N-terminal glutamine residues is accomplished by glutaminyl cyclase enzymes (EC 2.3.2.5). While in mammals these enzymes are involved in the synthesis of hormonal and neurotransmitter peptides, the physiological role played by the corresponding plant enzymes still remains to be unravelled. Papaya glutaminyl cyclase (PQC), a 33 kDa enzyme found in the latex of the tropical tree Carica papaya, displays an exceptional resistance to chemical and thermal denaturation as well as to proteolysis. In order to elucidate its enzymatic mechanism and to gain insights into the structural determinants underlying its remarkable stability, PQC was isolated from papaya latex, purified and crystallized by the hanging-drop vapour-diffusion method. The crystals belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 62.82, b = 81.23, c = 108.17 Å and two molecules per asymmetric unit. Diffraction data have been collected at ESRF beamline BM14 and processed to a resolution of 1.7 Å.},
doi = {10.1107/S1744309104025904},
journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 1,
volume = 61,
place = {United Kingdom},
year = {2005},
month = {1}
}