1jdi

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(New page: 200px<br /><applet load="1jdi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdi, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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caption="1jdi, resolution 2.4&Aring;" />
caption="1jdi, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE'''<br />
'''CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE'''<br />
==Overview==
==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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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==
==About this Structure==
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1JDI 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JDI OCA].
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1JDI 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 <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDI OCA].
==Reference==
==Reference==
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[[Category: L-ribulose-5-phosphate 4-epimerase]]
[[Category: L-ribulose-5-phosphate 4-epimerase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lee, J.E.]]
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[[Category: Lee, J E.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
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[[Category: Mosimann, S.C.]]
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[[Category: Mosimann, S C.]]
[[Category: Samuel, J.]]
[[Category: Samuel, J.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
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[[Category: Tanner, M.E.]]
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[[Category: Tanner, M E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: aldolase]]
[[Category: aldolase]]
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[[Category: ribulose]]
[[Category: ribulose]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:08:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:24 2008''

Revision as of 11:21, 21 February 2008


1jdi, resolution 2.4Å

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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

1JDI is a Single protein structure of sequence from Escherichia coli with as ligand. Active as L-ribulose-5-phosphate 4-epimerase, with EC number 5.1.3.4 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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