3bsy: Difference between revisions

Latest revision as of 12:13, 30 August 2023

PglD from Campylobacter jejuni, NCTC 11168, in complex with acetyl coenzyme A

Structural highlights

3bsy is a 3 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:	ACO
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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:https://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:https://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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1021/bi061456h

[2] 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:https://dx.doi.org/10.1139/o09-002

[3] 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

[1]

[2]

[3]

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3bsy]] is a 3 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=3BSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BSY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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]] 1.8&#8491;</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]], [[3bss|3bss]], [[3bsw|3bsw]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</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 jejuni])</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=3bsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bsy OCA], [https://pdbe.org/3bsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bsy RCSB], [https://www.ebi.ac.uk/pdbsum/3bsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bsy ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 35: @@
 [[Category: Campylobacter jejuni]]
 [[Category: Large Structures]]
-[[Category: UDP-N-acetylglucosamine diphosphorylase]]
+[[Category: Imperiali B]]
-[[Category: Imperiali, B]]
+[[Category: Olivier NB]]
-[[Category: Olivier, N B]]
-[[Category: Acetyl coenzyme some]]
-[[Category: Bacillosamine]]
-[[Category: Hexapeptide repeat]]
-[[Category: Left-hand beta helix]]
-[[Category: N-linked glycosylation]]
-[[Category: Pgl]]
-[[Category: Rossmann fold]]
-[[Category: Transferase]]
-[[Category: Udp]]

3bsy: Difference between revisions

Latest revision as of 12:13, 30 August 2023

PglD from Campylobacter jejuni, NCTC 11168, in complex with acetyl coenzyme A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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