4fwu: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q9VRQ9_DROME Q9VRQ9_DROME]  
[https://www.uniprot.org/uniprot/QPCT1_DROME QPCT1_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]<ref>PMID:17722885</ref> <ref>PMID:22897232</ref>
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== Publication Abstract from PubMed ==
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 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<ref>PMID:23545638</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[Glutaminyl cyclase|Glutaminyl cyclase]]
*[[Glutaminyl cyclase|Glutaminyl cyclase]]
== References ==
<references/>
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Latest revision as of 10:52, 6 November 2024

Crystal structure of glutaminyl cyclase from drosophila melanogaster in space group I4

4fwu, resolution 2.00Å

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