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| | ==Crystal structure of glutaminyl cyclase from drosophila melanogaster in space group I4== | | ==Crystal structure of glutaminyl cyclase from drosophila melanogaster in space group I4== |
| - | <StructureSection load='4fwu' size='340' side='right' caption='[[4fwu]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4fwu' size='340' side='right'caption='[[4fwu]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fwu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FWU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FWU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fwu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FWU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f9u|4f9u]], [[4f9v|4f9v]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">QC, CG10487, CG32412, Dmel_CG32412 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwu OCA], [https://pdbe.org/4fwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fwu RCSB], [https://www.ebi.ac.uk/pdbsum/4fwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fwu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fwu OCA], [http://pdbe.org/4fwu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fwu RCSB], [http://www.ebi.ac.uk/pdbsum/4fwu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fwu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4fwu" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4fwu" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glutaminyl cyclase|Glutaminyl cyclase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Koch, B]] | + | [[Category: Large Structures]] |
| - | [[Category: Kolenko, P]] | + | [[Category: Koch B]] |
| - | [[Category: Stubbs, M T]] | + | [[Category: Kolenko P]] |
| - | [[Category: Alpha/beta hydrolase]] | + | [[Category: Stubbs MT]] |
| - | [[Category: Alzheimer`s disease]]
| + | |
| - | [[Category: Glycosylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pglu formation]]
| + | |
| - | [[Category: Pglu-amyloid]]
| + | |
| - | [[Category: Pyroglutamate]]
| + | |
| Structural highlights
4fwu is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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][1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schilling S, Lindner C, Koch B, Wermann M, Rahfeld JU, von Bohlen A, Rudolph T, Reuter G, Demuth HU. Isolation and characterization of glutaminyl cyclases from Drosophila: evidence for enzyme forms with different subcellular localization. Biochemistry. 2007 Sep 25;46(38):10921-30. PMID:17722885 doi:10.1021/bi701043x
- ↑ Koch B, Kolenko P, Buchholz M, Ruiz Carrillo D, Parthier C, Wermann M, Rahfeld JU, Reuter G, Schilling S, Stubbs MT, Demuth HU. Crystal Structures of Glutaminyl Cyclases from Drosophila melanogaster Reveal Active Site Conservation between Insect and Mammalian QCs. Biochemistry. 2012 Aug 16. PMID:22897232 doi:10.1021/bi300687g
- ↑ Kolenko P, Koch B, Rahfeld JU, Schilling S, Demuth HU, Stubbs MT. Structure of glutaminyl cyclase from Drosophila melanogaster in space group I4. 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 doi:http://dx.doi.org/10.1107/S1744309113005575
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