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| | <StructureSection load='3bss' size='340' side='right'caption='[[3bss]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3bss' size='340' side='right'caption='[[3bss]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UD4:UDP-2-ACETAMIDO-4-AMINO-2,4,6-TRIDEOXY-ALPHA-D-GLUCOPYRANOSE'>UD4</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2npo|2npo]], [[3bsw|3bsw]], [[3bsy|3bsy]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UD4:UDP-2-ACETAMIDO-4-AMINO-2,4,6-TRIDEOXY-ALPHA-D-GLUCOPYRANOSE'>UD4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pglD ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase UDP-N-acetylglucosamine diphosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.23 2.7.7.23] </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=3bss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bss OCA], [https://pdbe.org/3bss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bss RCSB], [https://www.ebi.ac.uk/pdbsum/3bss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bss 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=3bss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bss OCA], [https://pdbe.org/3bss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bss RCSB], [https://www.ebi.ac.uk/pdbsum/3bss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bss ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PGLD_CAMJE PGLD_CAMJE]] Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.<ref>PMID:17087520</ref> <ref>PMID:19448740</ref>
| + | [https://www.uniprot.org/uniprot/PGLD_CAMJE PGLD_CAMJE] Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.<ref>PMID:17087520</ref> <ref>PMID:19448740</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter fetus subsp. jejuni smibert 1974]] | + | [[Category: Campylobacter jejuni]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UDP-N-acetylglucosamine diphosphorylase]]
| + | [[Category: Imperiali B]] |
| - | [[Category: Imperiali, B]] | + | [[Category: Olivier NB]] |
| - | [[Category: Olivier, N B]] | + | |
| - | [[Category: Acetyl coenzyme z]]
| + | |
| - | [[Category: Bacillosamine]]
| + | |
| - | [[Category: Campylobacter]]
| + | |
| - | [[Category: Hexapeptide repeat]]
| + | |
| - | [[Category: Left-hand beta helix]]
| + | |
| - | [[Category: N-linked glycosylation]]
| + | |
| - | [[Category: Pgl]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Udp]]
| + | |
| Structural highlights
Function
PGLD_CAMJE Acetyltransferase that modifies the UDP-4-amino-sugar to form UDP-N,N'-diacetylbacillosamine in the N-linked protein glycosylation pathway.[1] [2]
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 PubMed
The carbohydrate 2, 4-diacetamido-2, 4, 6-trideoxy-alpha-D-glucopyranose (BacAc(2)) is found in a variety of eubacterial pathogens. In Campylobacter jejuni, PglD acetylates the C4 amino group on UDP-2-acetamido-4-amino-2, 4, 6-trideoxy-alpha-D-glucopyranose (UDP-4-amino-sugar) to form UDP-BacAc(2). Sequence analysis predicts PglD to be a member of the left-handed beta helix family of enzymes. However, poor sequence homology between PglD and left-handed beta helix enzymes with existing structural data precludes unambiguous identification of the active site. The co-crystal structures of PglD in the presence of citrate, acetyl coenzyme A, or the UDP-4-amino-sugar were solved. The biological assembly is a trimer with one active site formed between two protomers. Residues lining the active site were identified, and results from functional assays on alanine mutants suggest His-125 is critical for catalysis, whereas His-15 and His-134 are involved in substrate binding. These results are discussed in the context of implications for proteins homologous to PglD in other pathogens.
Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni.,Olivier NB, Imperiali B J Biol Chem. 2008 Oct 10;283(41):27937-46. Epub 2008 Jul 30. PMID:18667421[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Olivier NB, Chen MM, Behr JR, Imperiali B. In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry. 2006 Nov 14;45(45):13659-69. PMID:17087520 doi:http://dx.doi.org/10.1021/bi061456h
- ↑ Demendi M, Creuzenet C. Cj1123c (PglD), a multifaceted acetyltransferase from Campylobacter jejuni. Biochem Cell Biol. 2009 Jun;87(3):469-83. doi: 10.1139/o09-002. PMID:19448740 doi:http://dx.doi.org/10.1139/o09-002
- ↑ Olivier NB, Imperiali B. Crystal structure and catalytic mechanism of PglD from Campylobacter jejuni. J Biol Chem. 2008 Oct 10;283(41):27937-46. Epub 2008 Jul 30. PMID:18667421 doi:10.1074/jbc.M801207200
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