4fwu: Difference between revisions

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</table>

== 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>

== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Glutaminyl cyclase|Glutaminyl cyclase]]

== References ==

__TOC__

</StructureSection>

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@@ Line 9: / Line 9: @@
 </table>
 == 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>
+<div style="background-color:#fffaf0;">
+== 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>
+</div>
+<div class="pdbe-citations 4fwu" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Glutaminyl cyclase|Glutaminyl cyclase]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>