3ru7: Difference between revisions

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New page: '''Unreleased structure''' The entry 3ru7 is ON HOLD Authors: Bhatt, V.S., Guan, W., Wang, P.G Description: Specific recognition of N-acetylated substrates and domain flexibility in Wb...
 
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'''Unreleased structure'''


The entry 3ru7 is ON HOLD
==Specific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimerase==
 
<StructureSection load='3ru7' size='340' side='right'caption='[[3ru7]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
Authors: Bhatt, V.S., Guan, W., Wang, P.G
== Structural highlights ==
 
<table><tr><td colspan='2'>[[3ru7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plesiomonas_shigelloides Plesiomonas shigelloides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RU7 FirstGlance]. <br>
Description: Specific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimerase
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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=3ru7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ru7 OCA], [https://pdbe.org/3ru7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ru7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ru7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ru7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GNE_PLESH GNE_PLESH] Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc). Has very low epimerase activity with UDP-Glc and UDP-Gal. Plays a role in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid, a building block of the O-antigen in bacterial lipopolysaccharide (LPS).<ref>PMID:12484781</ref> <ref>PMID:21810411</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plesiomonas shigelloides]]
[[Category: Bhatt VS]]
[[Category: Guan W]]
[[Category: Wang PG]]

Latest revision as of 15:37, 14 March 2024

Specific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimeraseSpecific recognition of N-acetylated substrates and domain flexibility in WbgU: a UDP-GalNAc 4-epimerase

Structural highlights

3ru7 is a 4 chain structure with sequence from Plesiomonas shigelloides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GNE_PLESH Catalyzes the epimerization of UDP-N-acetylglucosamine (UDP-GlcNAc) to UDP-N-acetylgalactosamine (UDP-GalNAc). Has very low epimerase activity with UDP-Glc and UDP-Gal. Plays a role in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid, a building block of the O-antigen in bacterial lipopolysaccharide (LPS).[1] [2]

References

  1. Kowal P, Wang PG. New UDP-GlcNAc C4 epimerase involved in the biosynthesis of 2-acetamino-2-deoxy-L-altruronic acid in the O-antigen repeating units of Plesiomonas shigelloides O17. Biochemistry. 2002 Dec 24;41(51):15410-4. PMID:12484781 doi:10.1021/bi026384i
  2. Bhatt VS, Guan W, Xue M, Yuan H, Wang PG. Insights into role of the hydrogen bond networks in substrate recognition by UDP-GalNAc 4-epimerases. Biochem Biophys Res Commun. 2011 Aug 26;412(2):232-7. PMID:21810411 doi:10.1016/j.bbrc.2011.07.071

3ru7, resolution 2.60Å

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