1lrj: Difference between revisions

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-[[Image:1lrj.jpg|left|200px]]<br /><applet load="1lrj" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1lrj, resolution 1.90&Aring;" />
-'''Crystal Structure of E. coli UDP-Galactose 4-Epimerase Complexed with UDP-N-Acetylglucosamine'''<br />
-==Overview==
+==Crystal Structure of E. coli UDP-Galactose 4-Epimerase Complexed with UDP-N-Acetylglucosamine==
-UDP-galactose 4-epimerase catalyzes the interconversion of UDP-Gal and, UDP-Glc during normal galactose metabolism. The mammalian form of the, enzyme, unlike its Escherichia coli counterpart, can also interconvert, UDP-GalNAc and UDP-GlcNAc. One key feature of the epimerase reaction, mechanism is the rotation of a 4-ketopyranose intermediate in the active, site. By comparing the high resolution x-ray structures of both the, bacterial and human forms of the enzyme, it was previously postulated that, the additional activity in the human epimerase was due to replacement of, the structural equivalent of Tyr-299 in the E. coli enzyme with a cysteine, residue, thereby leading to a larger active site volume. To test this, hypothesis, the Y299C mutant form of the E. coli enzyme was prepared and, its three-dimensional structure solved as described here. Additionally, the Y299C mutant protein was assayed for activity against both UDP-Gal and, UDP-GalNAc. These studies have revealed that, indeed, this simple mutation, did confer UDP-GalNAc/UDP-GlcNAc converting activity to the bacterial, enzyme with minimal changes in its three-dimensional structure., Specifically, although the Y299C mutation in the bacterial enzyme resulted, in a loss of epimerase activity with regard to UDP-Gal by almost 5-fold, it resulted in a gain of activity against UDP-GalNAc by more than, 230-fold.
+<StructureSection load='1lrj' size='340' side='right'caption='[[1lrj]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1lrj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LRJ 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=1lrj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lrj OCA], [https://pdbe.org/1lrj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lrj RCSB], [https://www.ebi.ac.uk/pdbsum/1lrj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lrj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GALE_ECOLI GALE_ECOLI]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lr/1lrj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=1lrj ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-LRJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA, NAD, UD1 and PGE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LRJ OCA].
+*[[UDP-galactose 4-epimerase|UDP-galactose 4-epimerase]]
+__TOC__
-==Reference==
+</StructureSection>
-Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks., Thoden JB, Henderson JM, Fridovich-Keil JL, Holden HM, J Biol Chem. 2002 Jul 26;277(30):27528-34. Epub 2002 May 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12019271 12019271]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: UDP-glucose 4-epimerase]]
+[[Category: Fridovich-Keil JL]]
-[[Category: Fridovich-Keil, J.L.]]
+[[Category: Henderson JM]]
-[[Category: Henderson, J.M.]]
+[[Category: Holden HM]]
-[[Category: Holden, H.M.]]
+[[Category: Thoden JB]]
-[[Category: Thoden, J.B.]]
-[[Category: NA]]
-[[Category: NAD]]
-[[Category: PGE]]
-[[Category: UD1]]
-[[Category: epimerase]]
-[[Category: galactosemia]]
-[[Category: short chain dehydrogenase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:48:40 2007''