4ztc: Difference between revisions

Revision as of 07:40, 18 May 2023

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

Structural highlights

4ztc is a 1 chain structure with sequence from Campylobacter jejuni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	4RA
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PGLE_CAMJE Aminotransferase involved in the bacillosamine biosynthesis pathway by producing UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose), a precursor used in the production of the glycan component 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose. Required for host colonization and virulence. Involved in the N-linked protein glycosylation pathway.^[1] ^[2]

Publication Abstract from PubMed

N,N'-diacetylbacillosamine is a novel sugar that plays a key role in bacterial glycosylation. Three enzymes are required for its biosynthesis in Campylobacter jejuni starting from UDP-GlcNAc. The focus of this investigation, PglE, catalyzes the second step in the pathway. It is a PLP-dependent aminotransferase that converts UDP-2-acetamido-4-keto-2,4,6-trideoxy-d-glucose to UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-glucose. For this investigation, the structure of PglE in complex with an external aldimine was determined to a nominal resolution of 2.0 A. A comparison of its structure with those of other sugar aminotransferases reveals a remarkable difference in the manner by which PglE accommodates its nucleotide-linked sugar substrate. This article is protected by copyright. All rights reserved.

Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis.,Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM Protein Sci. 2015 Jul 14. doi: 10.1002/pro.2745. PMID:26178292^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J Biol Chem. 2006 Jan 13;281(2):723-32. Epub 2005 Nov 11. PMID:16286454 doi:https://dx.doi.org/10.1074/jbc.M511021200
↑ Vijayakumar S, Merkx-Jacques A, Ratnayake DB, Gryski I, Obhi RK, Houle S, Dozois CM, Creuzenet C. Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential for protein glycosylation and virulence in Campylobacter jejuni. J Biol Chem. 2006 Sep 22;281(38):27733-43. PMID:16690622 doi:10.1074/jbc.M511714200
↑ Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM. Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis. Protein Sci. 2015 Jul 14. doi: 10.1002/pro.2745. PMID:26178292 doi:https://dx.doi.org/10.1002/pro.2745

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Schoenhofen IC, McNally DJ, Vinogradov E, Whitfield D, Young NM, Dick S, Wakarchuk WW, Brisson JR, Logan SM. Functional characterization of dehydratase/aminotransferase pairs from Helicobacter and Campylobacter: enzymes distinguishing the pseudaminic acid and bacillosamine biosynthetic pathways. J Biol Chem. 2006 Jan 13;281(2):723-32. Epub 2005 Nov 11. PMID:16286454 doi:https://dx.doi.org/10.1074/jbc.M511021200

[2] Vijayakumar S, Merkx-Jacques A, Ratnayake DB, Gryski I, Obhi RK, Houle S, Dozois CM, Creuzenet C. Cj1121c, a novel UDP-4-keto-6-deoxy-GlcNAc C-4 aminotransferase essential for protein glycosylation and virulence in Campylobacter jejuni. J Biol Chem. 2006 Sep 22;281(38):27733-43. PMID:16690622 doi:10.1074/jbc.M511714200

[3] Riegert AS, Young NM, Watson DC, Thoden JB, Holden HM. Structure of the external aldimine form of PglE, an aminotransferase required for N,N'-diacetylbacillosamine biosynthesis. Protein Sci. 2015 Jul 14. doi: 10.1002/pro.2745. PMID:26178292 doi:https://dx.doi.org/10.1002/pro.2745

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='4ztc' size='340' side='right'caption='[[4ztc]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ztc]] is a 1 chain structure with sequence from [http://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=4ZTC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZTC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ztc]] 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=4ZTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZTC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4RA:[(2R,3R,4R,5S,6R)-3-ACETAMIDO-6-METHYL-5-[(E)-[2-METHYL-3-OXIDANYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]-4-OXIDANYL-OXAN-2-YL]+[[(2R,3S,4R,5R)-5-[2,4-BIS(OXIDANYLIDENE)PYRIMIDIN-1-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+HYDROGEN+PHOSPHATE'>4RA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4RA:[(2R,3R,4R,5S,6R)-3-ACETAMIDO-6-METHYL-5-[(E)-[2-METHYL-3-OXIDANYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]-4-OXIDANYL-OXAN-2-YL]+[[(2R,3S,4R,5R)-5-[2,4-BIS(OXIDANYLIDENE)PYRIMIDIN-1-YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+HYDROGEN+PHOSPHATE'>4RA</scene></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=4ztc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ztc OCA], [http://pdbe.org/4ztc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ztc RCSB], [http://www.ebi.ac.uk/pdbsum/4ztc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ztc 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=4ztc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ztc OCA], [https://pdbe.org/4ztc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ztc RCSB], [https://www.ebi.ac.uk/pdbsum/4ztc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ztc ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PGLE_CAMJE PGLE_CAMJE] Aminotransferase involved in the bacillosamine biosynthesis pathway by producing UDP-4-amino-4,6-dideoxy-alpha-D-GlcNAc (UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose), a precursor used in the production of the glycan component 2,4-diacetamido-2,4,6-trideoxy-alpha-D-glucopyranose. Required for host colonization and virulence. Involved in the N-linked protein glycosylation pathway.<ref>PMID:16286454</ref> <ref>PMID:16690622</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Campylobacter fetus subsp. jejuni smibert 1974]]
+[[Category: Campylobacter jejuni]]
 [[Category: Large Structures]]
-[[Category: Holden, H M]]
+[[Category: Holden HM]]
-[[Category: Riegert, A S]]
+[[Category: Riegert AS]]
-[[Category: Thoden, J B]]
+[[Category: Thoden JB]]
-[[Category: Watson, D C]]
+[[Category: Watson DC]]
-[[Category: Young, N M]]
+[[Category: Young NM]]
-[[Category: Aminotransferase]]
-[[Category: N-glycosylation pyridoxyl 5'-phosphate]]
-[[Category: N-n'-diacetylbacillosamine]]
-[[Category: Transferase]]

4ztc: Difference between revisions

Revision as of 07:40, 18 May 2023

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

Structural highlights

Function

Publication Abstract from PubMed

References

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