4ztc
From Proteopedia
(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. 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> | ||
+ | </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> | ||
+ | <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://www.rcsb.org/pdb/explore.do?structureId=4ztc RCSB], [http://www.ebi.ac.uk/pdbsum/4ztc PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <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> | |
- | + | </div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
- | [[Category: Riegert, A | + | __TOC__ |
- | [[Category: Thoden, J | + | </StructureSection> |
- | [[Category: | + | [[Category: Holden, H M]] |
- | [[Category: | + | [[Category: Riegert, A S]] |
- | [[Category: | + | [[Category: Thoden, J B]] |
+ | [[Category: Watson, D C]] | ||
+ | [[Category: Young, N M]] | ||
+ | [[Category: Aminotransferase]] | ||
+ | [[Category: N-glycosylation pyridoxyl 5'-phosphate]] | ||
+ | [[Category: N-n'-diacetylbacillosamine]] | ||
+ | [[Category: Transferase]] |
Revision as of 14:41, 29 July 2015
PglE Aminotransferase in complex with External Aldimine, Mutant K184A
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