1k0w
From Proteopedia
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|PDB= 1k0w |SIZE=350|CAPTION= <scene name='initialview01'>1k0w</scene>, resolution 2.10Å | |PDB= 1k0w |SIZE=350|CAPTION= <scene name='initialview01'>1k0w</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= ARAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ARAD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jdi|1JDI]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0w OCA], [http://www.ebi.ac.uk/pdbsum/1k0w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k0w RCSB]</span> | ||
}} | }} | ||
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[[Category: Samuel, J.]] | [[Category: Samuel, J.]] | ||
[[Category: Strynadka, N C.J.]] | [[Category: Strynadka, N C.J.]] | ||
| - | [[Category: ZN]] | ||
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: epimerase]] | [[Category: epimerase]] | ||
[[Category: ribulose]] | [[Category: ribulose]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:41:46 2008'' |
Revision as of 18:41, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ARAD (Escherichia coli) | ||||||
| Activity: | L-ribulose-5-phosphate 4-epimerase, with EC number 5.1.3.4 | ||||||
| Related: | 1JDI
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE
Overview
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.
About this Structure
1K0W is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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