3vu1: Difference between revisions
No edit summary |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (PhAglB-L, O74088_PYRHO) from Pyrococcus horikoshii== | |||
<StructureSection load='3vu1' size='340' side='right'caption='[[3vu1]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vu1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VU1 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3vu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vu1 OCA], [https://pdbe.org/3vu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vu1 RCSB], [https://www.ebi.ac.uk/pdbsum/3vu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vu1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AGLB1_PYRHO AGLB1_PYRHO] Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in Pyrococcus) 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.[UniProtKB:Q8U4D2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Oligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the +2 position in the N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by (15)N NMR relaxation analyses. Intriguingly, the mobile region contains the +2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide crosslink abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains. | |||
Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.,Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F, Kohda D Structure. 2013 Jan 8;21(1):32-41. doi: 10.1016/j.str.2012.10.011. Epub 2012 Nov , 21. PMID:23177926<ref>PMID:23177926</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vu1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Inagaki F]] | |||
[[Category: Kohda D]] | |||
[[Category: Maita N]] | |||
[[Category: Matsumoto S]] | |||
[[Category: Noda NN]] | |||
[[Category: Nyirenda J]] | |||
[[Category: Saitoh T]] | |||
Latest revision as of 15:37, 8 November 2023
Crystal structure of the C-terminal globular domain of oligosaccharyltransferase (PhAglB-L, O74088_PYRHO) from Pyrococcus horikoshiiCrystal structure of the C-terminal globular domain of oligosaccharyltransferase (PhAglB-L, O74088_PYRHO) from Pyrococcus horikoshii
Structural highlights
FunctionAGLB1_PYRHO Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (ManNAcXyl(2)GlcAMan(2)GalNAc in Pyrococcus) 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.[UniProtKB:Q8U4D2] Publication Abstract from PubMedOligosaccharyltransferase (OST) is a membrane-bound enzyme that catalyzes the transfer of an oligosaccharide to an asparagine residue in glycoproteins. It possesses a binding pocket that recognizes Ser and Thr residues at the +2 position in the N-glycosylation consensus, Asn-X-Ser/Thr. We determined the crystal structures of the C-terminal globular domains of the catalytic subunits of two archaeal OSTs. A comparison with previously determined structures identified a segment with remarkable conformational plasticity, induced by crystal contact effects. We characterized its dynamic properties in solution by (15)N NMR relaxation analyses. Intriguingly, the mobile region contains the +2 Ser/Thr-binding pocket. In agreement, the flexibility restriction forced by an engineered disulfide crosslink abolished the enzymatic activity, and its cleavage fully restored activity. These results suggest the necessity of multiple conformational states in the reaction. The dynamic nature of the Ser/Thr pocket could facilitate the efficient scanning of N-glycosylation sequons along nascent polypeptide chains. Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.,Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F, Kohda D Structure. 2013 Jan 8;21(1):32-41. doi: 10.1016/j.str.2012.10.011. Epub 2012 Nov , 21. PMID:23177926[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||