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| | <StructureSection load='1k0w' size='340' side='right'caption='[[1k0w]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='1k0w' size='340' side='right'caption='[[1k0w]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k0w]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1K0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1k0w]] is a 6 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=1K0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jdi|1jdi]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1k0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0w OCA], [https://pdbe.org/1k0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0w RCSB], [https://www.ebi.ac.uk/pdbsum/1k0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0w ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-ribulose-5-phosphate_4-epimerase L-ribulose-5-phosphate 4-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.4 5.1.3.4] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1k0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0w OCA], [http://pdbe.org/1k0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k0w RCSB], [http://www.ebi.ac.uk/pdbsum/1k0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ARAD_ECOLI ARAD_ECOLI] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: L-ribulose-5-phosphate 4-epimerase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lee, J E]] | + | [[Category: Lee JE]] |
| - | [[Category: Luo, Y]] | + | [[Category: Luo Y]] |
| - | [[Category: Mosimann, S C]] | + | [[Category: Mosimann SC]] |
| - | [[Category: Samuel, J]] | + | [[Category: Samuel J]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: Epimerase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Ribulose]]
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| Structural highlights
Function
ARAD_ECOLI
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 PubMed
The structure of L-ribulose-5-phosphate 4-epimerase from E. coli has been solved to 2.4 A resolution using X-ray diffraction data. The structure is homo-tetrameric and displays C(4) symmetry. Each subunit has a single domain comprised of a central beta-sheet flanked on either side by layers of alpha-helices. The active site is identified by the position of the catalytic zinc residue and is located at the interface between two adjacent subunits. A remarkable feature of the structure is that it shows a very close resemblance to that of L-fuculose-1-phosphate aldolase. This is consistent with the notion that both enzymes belong to a superfamily of epimerases/aldolases that catalyze carbon-carbon bond cleavage reactions via a metal-stabilized enolate intermediate. Detailed inspection of the epimerase structure, however, indicates that despite the close overall structural similarity to class II aldolases, the enzyme has evolved distinct active site features that promote its particular chemistry.
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.,Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC Biochemistry. 2001 Dec 11;40(49):14763-71. PMID:11732895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC. The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization. Biochemistry. 2001 Dec 11;40(49):14763-71. PMID:11732895
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