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| | <StructureSection load='3wai' size='340' side='right'caption='[[3wai]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3wai' size='340' side='right'caption='[[3wai]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WAI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wai]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WAI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3waj|3waj]], [[3wak|3wak]]</div></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]] 1.897Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, aglB-L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3wai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wai OCA], [https://pdbe.org/3wai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wai RCSB], [https://www.ebi.ac.uk/pdbsum/3wai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wai ProSAT]</span></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=3wai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wai OCA], [https://pdbe.org/3wai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wai RCSB], [https://www.ebi.ac.uk/pdbsum/3wai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wai ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
| + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/AGLB3_ARCFU AGLB3_ARCFU] Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.<ref>PMID:24127570</ref> <ref>PMID:27015803</ref> <ref>PMID:27997792</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 3wai" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3wai" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Archaeoglobus fulgidus DSM 4304]] |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kohda, D]] | + | [[Category: Kohda D]] |
| - | [[Category: Matsumoto, S]] | + | [[Category: Matsumoto S]] |
| - | [[Category: Shimada, A]] | + | [[Category: Shimada A]] |
| - | [[Category: Gt-c]]
| + | |
| - | [[Category: Mbp fusion]]
| + | |
| - | [[Category: N-glycosylation]]
| + | |
| - | [[Category: Oligosaccharyltransferase]]
| + | |
| - | [[Category: Protein b-oligosaccharyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.AGLB3_ARCFU Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a glucose-linked heptasaccharide composed of 3 Glc, 2 Man, 2 Gal and a sulfate for A.fulgidus AglB-L) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation.[1] [2] [3]
Publication Abstract from PubMed
BACKGROUND: Protein N-glycosylation occurs in the three domains of life. Oligosaccharyltransferase (OST) transfers an oligosaccharide chain to the asparagine residue in the N-glycosylation sequons. The catalytic subunits of the OST enzyme are STT3 in eukaryotes, AglB in archaea and PglB in eubacteria. The genome of a hyperthermophilic archaeon, Archaeoglobus fulgidus, encodes three paralogous AglB proteins. We previously solved the crystal structures of the C-terminal globular domains of two paralogs, AglB-Short 1 and AglB-Short 2. RESULTS: We determined the crystal structure of the C-terminal globular domain of the third AglB paralog, AglB-Long, at 1.9 A resolutions. The crystallization of the fusion protein with maltose binding protein (MBP) afforded high quality protein crystals. Two MBP-AglB-L molecules formed a swapped dimer in the crystal. Since the fusion protein behaved as a monomer upon gel filtration, we reconstituted the monomer structure from the swapped dimer by exchanging the swapped segments. The C-terminal domain of A. fulgidus AglB-L includes a structural unit common to AglB-S1 and AglB-S2. This structural unit contains the evolutionally conserved WWDYG and DK motifs. The present structure revealed that A. fulgidus AglB-L contained a variant type of the DK motif with a short insertion, and confirmed that the second signature residue, Lys, of the DK motif participates in the formation of a pocket that binds to the serine and threonine residues at the +2 position of the N-glycosylation sequon. CONCLUSIONS: The structure of A. fulgidus AglB-L, together with the two previously solved structures of AglB-S1 and AglB-S2, provides a complete overview of the three AglB paralogs encoded in the A. fulgidus genome. All three AglBs contain a variant type of the DK motif. This finding supports a previously proposed rule: The STT3/AglB/PglB paralogs in one organism always contain the same type of Ser/Thr-binding pocket. The present structure will be useful as a search model for molecular replacement in the structural determination of the full-length A. fulgidus AglB-L.
Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases.,Matsumoto S, Shimada A, Kohda D BMC Struct Biol. 2013 Jul 1;13(1):11. PMID:23815857[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsumoto S, Shimada A, Nyirenda J, Igura M, Kawano Y, Kohda D. Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Proc Natl Acad Sci U S A. 2013 Oct 14. PMID:24127570 doi:http://dx.doi.org/10.1073/pnas.1309777110
- ↑ Taguchi Y, Fujinami D, Kohda D. Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation. J Biol Chem. 2016 May 20;291(21):11042-54. PMID:27015803 doi:10.1074/jbc.M115.713156
- ↑ Matsumoto S, Taguchi Y, Shimada A, Igura M, Kohda D. Tethering an N-Glycosylation Sequon-Containing Peptide Creates a Catalytically Competent Oligosaccharyltransferase Complex. Biochemistry. 2017 Jan 31;56(4):602-611. doi: 10.1021/acs.biochem.6b01089. Epub, 2017 Jan 17. PMID:27997792 doi:http://dx.doi.org/10.1021/acs.biochem.6b01089
- ↑ Matsumoto S, Shimada A, Kohda D. Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases. BMC Struct Biol. 2013 Jul 1;13(1):11. PMID:23815857 doi:10.1186/1472-6807-13-11
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