2zag: Difference between revisions
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==Crystal structure of the SeMet-substituted soluble domain of STT3 from P. furiosus== | ==Crystal structure of the SeMet-substituted soluble domain of STT3 from P. furiosus== | ||
<StructureSection load='2zag' size='340' side='right' caption='[[2zag]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='2zag' size='340' side='right' caption='[[2zag]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zai|2zai]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zai|2zai]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0156 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</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=2zag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zag OCA], [http://pdbe.org/2zag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zag RCSB], [http://www.ebi.ac.uk/pdbsum/2zag PDBsum]</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=2zag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zag OCA], [http://pdbe.org/2zag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zag RCSB], [http://www.ebi.ac.uk/pdbsum/2zag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zag ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zag_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zag_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:24, 17 October 2018
Crystal structure of the SeMet-substituted soluble domain of STT3 from P. furiosusCrystal structure of the SeMet-substituted soluble domain of STT3 from P. furiosus
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAsn-glycosylation is widespread not only in eukaryotes but also in archaea and some eubacteria. Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. Here, we report that a thermophilic archaeon, Pyrococcus furiosus OST is composed of the STT3 protein alone, and catalyzes the transfer of a heptasaccharide, containing one hexouronate and two pentose residues, onto peptides in an Asn-X-Thr/Ser-motif-dependent manner. We also determined the 2.7-A resolution crystal structure of the C-terminal soluble domain of Pyrococcus STT3. The structure-based multiple sequence alignment revealed a new motif, DxxK, which is adjacent to the well-conserved WWDYG motif in the tertiary structure. The mutagenesis of the DK motif residues in yeast STT3 revealed the essential role of the motif in the catalytic activity. The function of this motif may be related to the binding of the pyrophosphate group of lipid-linked oligosaccharide donors through a transiently bound cation. Our structure provides the first structural insights into the formation of the oligosaccharide-asparagine bond. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase.,Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K, Kohda D EMBO J. 2008 Jan 9;27(1):234-43. Epub 2007 Nov 29. PMID:18046457[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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