4mo2: Difference between revisions
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==Crystal Structure of UDP-N-acetylgalactopyranose mutase from Campylobacter jejuni== | ==Crystal Structure of UDP-N-acetylgalactopyranose mutase from Campylobacter jejuni== | ||
<StructureSection load='4mo2' size='340' side='right' caption='[[4mo2]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4mo2' size='340' side='right'caption='[[4mo2]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mo2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mo2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni_subsp._jejuni_NCTC_11168_=_ATCC_700819 Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MO2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4mo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mo2 OCA], [https://pdbe.org/4mo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mo2 RCSB], [https://www.ebi.ac.uk/pdbsum/4mo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mo2 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0P8H5_CAMJE Q0P8H5_CAMJE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4mo2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4mo2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[UDP-galactopyranose mutase 3D structures|UDP-galactopyranose mutase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Dalrymple | [[Category: Dalrymple SA]] | ||
[[Category: Lowary | [[Category: Lowary TL]] | ||
[[Category: Poulin | [[Category: Poulin MB]] | ||
[[Category: Protsko | [[Category: Protsko C]] | ||
[[Category: Sanders | [[Category: Sanders DAR]] | ||
Revision as of 12:57, 28 December 2022
Crystal Structure of UDP-N-acetylgalactopyranose mutase from Campylobacter jejuniCrystal Structure of UDP-N-acetylgalactopyranose mutase from Campylobacter jejuni
Structural highlights
FunctionPublication Abstract from PubMedPyranose-furanose mutases are essential enzymes in the life cycle of a number of microorganisms, but are absent in mammalian systems, and hence represent novel targets for drug development. To date, all such mutases show preferential recognition of a single substrate (e.g., UDP-Gal). We report here the detailed structural characterization of the first bifunctional pyranose-furanose mutase, which recognizes both UDP-Gal and UDP-GalNAc. The enzyme under investigation (cjUNGM) is involved in the biosynthesis of capsular polysaccharides (CPSs) in Campylobacter jejuni 11168. These CPSs are known virulence factors that are required for adhesion and invasion of human epithelial cells. Using a combination of UV/visible spectroscopy, X-ray crystallography, saturation transfer difference NMR spectroscopy, molecular dynamics and CORCEMA-ST calculations, we have characterized the binding of the enzyme to both UDP-Galp and UDP-GalpNAc, and compared these interactions with those of a homologous monofunctional mutase enzyme from E. coli (ecUGM). These studies reveal that two arginines in cjUNGM, Arg59 and Arg168, play critical roles in the catalytic mechanism of the enzyme and in controlling its specificity to ultimately lead to a GalfNAc-containing CPS. In ecUGM, these arginines are replaced with histidine and lysine, respectively, and this results in an enzyme that is selective for UDP-Gal. We propose that these changes in amino acids allow C. jejuni 11168 to produce suitable quantities of the sugar nucleotide substrate required for the assembly of a CPS containing GalfNAc, which is essential for viability. Specificity of a UDP-GalNAc Pyranose-Furanose Mutase: A Potential Therapeutic Target for Campylobacter jejuni Infections.,Poulin MB, Shi Y, Protsko C, Dalrymple SA, Sanders DA, Pinto BM, Lowary TL Chembiochem. 2014 Jan 3;15(1):47-56. doi: 10.1002/cbic.201300653. Epub 2013 Dec, 2. PMID:24302429[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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