1jdi

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{{STRUCTURE_1jdi| PDB=1jdi | SCENE= }}
{{STRUCTURE_1jdi| PDB=1jdi | SCENE= }}
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'''CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE'''
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===CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11732895 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11732895}}
==About this Structure==
==About this Structure==
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[[Category: Epimerase]]
[[Category: Epimerase]]
[[Category: Ribulose]]
[[Category: Ribulose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:05:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:04:33 2008''

Revision as of 17:04, 1 July 2008

Image:1jdi.png

Template:STRUCTURE 1jdi

CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE

Template:ABSTRACT PUBMED 11732895

About this Structure

1JDI 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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