Open AccessStructure of glutaminyl cyclase from Drosophila melanogaster in space group I 4
Author(s) -
Kolenko Petr,
Koch Birgit,
Rahfeld JensUlrich,
Schilling Stephan,
Demuth HansUlrich,
Stubbs Milton T.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113005575
Subject(s) - drosophila melanogaster , crystallography , group (periodic table) , ligand (biochemistry) , chemistry , crystal structure , resolution (logic) , hydrolase , crystal (programming language) , molecular replacement , stereochemistry , enzyme , biochemistry , receptor , gene , organic chemistry , artificial intelligence , computer science , programming language
The structure of ligand‐free glutaminyl cyclase (QC) from Drosophila melanogaster ( Dm QC) has been determined in a novel crystal form. The protein crystallized in space group I 4, with unit‐cell parameters a = b = 122.3, c = 72.7 Å. The crystal diffracted to a resolution of 2 Å at the home source. The structure was solved by molecular replacement and was refined to an R factor of 0.169. Dm QC exhibits a typical α/β‐hydrolase fold. The electron density of three monosaccharides could be localized. The accessibility of the active site will facilitate structural studies of novel inhibitor‐binding modes.