1a9y: Difference between revisions
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==UDP-GALACTOSE 4-EPIMERASE MUTANT S124A/Y149F COMPLEXED WITH UDP-GLUCOSE== | ==UDP-GALACTOSE 4-EPIMERASE MUTANT S124A/Y149F COMPLEXED WITH UDP-GLUCOSE== | ||
<StructureSection load='1a9y' size='340' side='right' caption='[[1a9y]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1a9y' size='340' side='right' caption='[[1a9y]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a9y]] is a 1 chain structure | <table><tr><td colspan='2'>[[1a9y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A9Y FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucose_4-epimerase UDP-glucose 4-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.2 5.1.3.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-glucose_4-epimerase UDP-glucose 4-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.2 5.1.3.2] </span></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=1a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a9y OCA], [http://pdbe.org/1a9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a9y RCSB], [http://www.ebi.ac.uk/pdbsum/1a9y PDBsum]</span></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=1a9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a9y OCA], [http://pdbe.org/1a9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1a9y RCSB], [http://www.ebi.ac.uk/pdbsum/1a9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1a9y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1a9y ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: UDP-glucose 4-epimerase]] | [[Category: UDP-glucose 4-epimerase]] | ||
[[Category: Holden, H M]] | [[Category: Holden, H M]] | ||
Revision as of 12:22, 9 August 2017
UDP-GALACTOSE 4-EPIMERASE MUTANT S124A/Y149F COMPLEXED WITH UDP-GLUCOSEUDP-GALACTOSE 4-EPIMERASE MUTANT S124A/Y149F COMPLEXED WITH UDP-GLUCOSE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUDP-galactose 4-epimerase catalyzes the interconversion of UDP-galactose and UDP-glucose during normal galactose metabolism. Within recent years the enzyme from Escherichia coli has been studied extensively by both biochemical and X-ray crystallographic techniques. One of several key features in the catalytic mechanism of the enzyme involves the putative rotation of a 4'-ketopyranose intermediate within the active site region. The mode of binding of UDP-glucose to epimerase is well understood on the basis of previous high-resolution X-ray crystallographic investigations from this laboratory with an enzyme/NADH/UDP-glucose abortive complex. Attempts to prepare an enzyme/NADH/UDP-galactose abortive complex always failed, however, in that UDP-glucose rather than UDP-galactose was observed binding in the active site. In an effort to prepare an abortive complex with UDP-galactose, a site-directed mutant protein was constructed in which Ser 124 and Tyr 149, known to play critical roles in catalysis, were substituted with alanine and phenylalanine residues, respectively. With this double mutant it was possible to crystallize and solve the three-dimensional structures of reduced epimerase in the presence of UDP-glucose or UDP-galactose to high resolution. This study represents the first direct observation of UDP-galactose binding to epimerase and lends strong structural support for a catalytic mechanism in which there is free rotation of a 4'-ketopyranose intermediate within the active site cleft of the enzyme. Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.,Thoden JB, Holden HM Biochemistry. 1998 Aug 18;37(33):11469-77. PMID:9708982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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