4ztc

From Proteopedia

(Difference between revisions)

Current revision

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.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
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:http://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:http://dx.doi.org/10.1002/pro.2745

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ztc"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4ztc is ON HOLD  until Paper Publication
+==PglE Aminotransferase in complex with External Aldimine, Mutant K184A==
+<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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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'>[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 ==
+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.
-Authors: Riegert, A.S., Thoden, J.B., Young, N.M., Watson, D.C., Holden, H.M.
+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<ref>PMID:26178292</ref>
-Description: PglE Aminotransferase in complex with External Aldimine, Mutant K184A
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Riegert, A.S]]
+<div class="pdbe-citations 4ztc" style="background-color:#fffaf0;"></div>
-[[Category: Thoden, J.B]]
+== References ==
-[[Category: Holden, H.M]]
+<references/>
-[[Category: Watson, D.C]]
+__TOC__
-[[Category: Young, N.M]]
+</StructureSection>
+[[Category: Campylobacter jejuni]]
+[[Category: Large Structures]]
+[[Category: Holden HM]]
+[[Category: Riegert AS]]
+[[Category: Thoden JB]]
+[[Category: Watson DC]]
+[[Category: Young NM]]

4ztc

From Proteopedia

Current revision

PglE Aminotransferase in complex with External Aldimine, Mutant K184A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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