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Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4.


ABSTRACT: The structure of ligand-free glutaminyl cyclase (QC) from Drosophila melanogaster (DmQC) has been determined in a novel crystal form. The protein crystallized in space group I4, 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. DmQC exhibits a typical ?/?-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.

SUBMITTER: Kolenko P 

PROVIDER: S-EPMC3614157 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4.

Kolenko Petr P   Koch Birgit B   Rahfeld Jens Ulrich JU   Schilling Stephan S   Demuth Hans Ulrich HU   Stubbs Milton T MT  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130328 Pt 4


The structure of ligand-free glutaminyl cyclase (QC) from Drosophila melanogaster (DmQC) has been determined in a novel crystal form. The protein crystallized in space group I4, 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. DmQC exhibits a typical α/β-hydrolase fold. The electron density of three monosaccharides could be localized. Th  ...[more]

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