1xel: Difference between revisions

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New page: left|200px<br /><applet load="1xel" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xel, resolution 1.8Å" /> '''UDP-GALACTOSE 4-EPIME...
 
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[[Image:1xel.jpg|left|200px]]<br /><applet load="1xel" size="450" color="white" frame="true" align="right" spinBox="true"
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'''UDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLI'''<br />


==Overview==
==UDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLI==
UDP-galactose 4-epimerase is one of three enzymes in the metabolic pathway, that converts galactose into glucose1-phosphate. Specifically this enzyme, catalyzes the interconversion of UDP-galactose and UDP-glucose. The, molecular structure of the NADH/UDP-glucose abortive complex of the enzyme, from Escherichia coli has been determined by X-ray diffraction analysis to, a nominal resolution of 1.8 A and refined to an R-factor of 18.2% for all, measurement X-ray data. The nicotinamide ring of the dinucleotide adopts, the syn conformation in relationship to the ribose. Both the NADH and, UDP-glucose are in the proper orientation for a B-side specific transfer, from C4 of the sugar to C4 of the dinucleotide. Those residues implicated, in glucose binding include Ser 124, tyr 149, Asn 179, Asn199, Arg 231, and, Tyr 299. An amino acid sequence alignment of various prokaryotic and, eukaryotic epimerases reveals a high degree of conservation with respect, to those residues involved in both NADH and substrate binding. The, nonstereospecificity displayed by epimerase was originally thought to, occur through a simple rotation about the bond between the glycosyl C1, oxygen of the 4-ketose intermediate and the beta-phosphorous of the UDP, moiety, thereby allowing the opposite side of the sugar to face the NADH., The present structure reveals that additional rotations about the, phosphate backbone of UDP are necessary. Furthermore, the abortive complex, model described here suggests that Ser 124 and Tyr 149 are likely to play, important roles in the catalytic mechanism of the enzyme.
<StructureSection load='1xel' size='340' side='right'caption='[[1xel]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xel]] 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=1XEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XEL 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</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=1xel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xel OCA], [https://pdbe.org/1xel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xel RCSB], [https://www.ebi.ac.uk/pdbsum/1xel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xel 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/xe/1xel_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=1xel ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1XEL 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, UPG, EDO and PEG 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=1XEL OCA].
*[[UDP-galactose 4-epimerase|UDP-galactose 4-epimerase]]
 
__TOC__
==Reference==
</StructureSection>
Molecular structure of the NADH/UDP-glucose abortive complex of UDP-galactose 4-epimerase from Escherichia coli: implications for the catalytic mechanism., Thoden JB, Frey PA, Holden HM, Biochemistry. 1996 Apr 23;35(16):5137-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8611497 8611497]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: UDP-glucose 4-epimerase]]
[[Category: Holden H]]
[[Category: Holden, H.]]
[[Category: Thoden J]]
[[Category: Thoden, J.]]
[[Category: EDO]]
[[Category: NA]]
[[Category: NAD]]
[[Category: PEG]]
[[Category: UPG]]
[[Category: isomerase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:01:27 2007''

Latest revision as of 11:49, 14 February 2024

UDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLIUDP-GALACTOSE 4-EPIMERASE FROM ESCHERICHIA COLI

Structural highlights

1xel is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GALE_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1xel, resolution 1.80Å

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