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| | <StructureSection load='1jdi' size='340' side='right'caption='[[1jdi]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1jdi' size='340' side='right'caption='[[1jdi]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1jdi]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JDI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1jdi]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDI 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]] 2.4Å</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=83333 ECOLI])</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=1jdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdi OCA], [https://pdbe.org/1jdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdi RCSB], [https://www.ebi.ac.uk/pdbsum/1jdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdi ProSAT]</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=1jdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdi OCA], [http://pdbe.org/1jdi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jdi RCSB], [http://www.ebi.ac.uk/pdbsum/1jdi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdi 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: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[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: Tanner, M E]] | + | [[Category: Tanner ME]] |
| - | [[Category: Aldolase]]
| + | |
| - | [[Category: Epimerase]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Ribulose]]
| + | |
| 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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