4ztc: Difference between revisions
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==PglE Aminotransferase in complex with External Aldimine, Mutant K184A== | |||
<StructureSection load='4ztc' size='340' side='right'caption='[[4ztc]], [[Resolution|resolution]] 2.00Å' 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]] 2Å</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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4ztc" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Watson | __TOC__ | ||
[[Category: Young | </StructureSection> | ||
[[Category: Campylobacter jejuni]] | |||
[[Category: Large Structures]] | |||
[[Category: Holden HM]] | |||
[[Category: Riegert AS]] | |||
[[Category: Thoden JB]] | |||
[[Category: Watson DC]] | |||
[[Category: Young NM]] | |||
Latest revision as of 08:23, 27 September 2023
PglE Aminotransferase in complex with External Aldimine, Mutant K184A
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