4fwu
From Proteopedia
Crystal structure of glutaminyl cyclase from drosophila melanogaster in space group I4
Structural highlights
FunctionQPCT1_DROME Acts as a glutaminyl-peptide cyclotransferase (PubMed:17722885, PubMed:22897232). Responsible for the biosynthesis of pyroglutamyl peptides (By similarity). Might be more efficient in the conversion of tri and tetrapeptides in vitro (PubMed:17722885). Might have a relative preference for substrates containing hydrophobic amino acids in vitro (PubMed:17722885).[UniProtKB:Q16769][1] [2] Publication Abstract from PubMedThe 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 A. The crystal diffracted to a resolution of 2 A 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 alpha/beta-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. Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4.,Kolenko P, Koch B, Rahfeld JU, Schilling S, Demuth HU, Stubbs MT Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Apr 1;69(Pt 4):358-61., doi: 10.1107/S1744309113005575. Epub 2013 Mar 28. PMID:23545638[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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