1dxf

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(New page: 200px<br /><applet load="1dxf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dxf, resolution 2.6&Aring;" /> '''2-DEHYDRO-3-DEOXY-GAL...)
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caption="1dxf, resolution 2.6&Aring;" />
caption="1dxf, resolution 2.6&Aring;" />
'''2-DEHYDRO-3-DEOXY-GALACTARATE ALDOLASE FROM ESCHERICHIA COLI IN COMPLEX WITH PYRUVATE'''<br />
'''2-DEHYDRO-3-DEOXY-GALACTARATE ALDOLASE FROM ESCHERICHIA COLI IN COMPLEX WITH PYRUVATE'''<br />
==Overview==
==Overview==
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Carbon-carbon bond formation is an essential reaction in organic chemistry, and the use of aldolase enzymes for the stereochemical control of such, reactions is an attractive alternative to conventional chemical methods., Here we describe the crystal structures of a novel class II enzyme, 2-dehydro-3-deoxy-galactarate (DDG) aldolase from Escherichia coli, in the, presence and absence of substrate. The crystal structure was determined by, locating only four Se sites to obtain phases for 506 protein residues. The, protomer displays a modified (alpha/beta)(8) barrel fold, in which the, eighth alpha-helix points away from the beta-barrel instead of packing, against it. Analysis of the DDG aldolase crystal structures suggests a, novel aldolase mechanism in which a phosphate anion accepts the proton, from the methyl group of pyruvate.
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Carbon-carbon bond formation is an essential reaction in organic chemistry and the use of aldolase enzymes for the stereochemical control of such reactions is an attractive alternative to conventional chemical methods. Here we describe the crystal structures of a novel class II enzyme, 2-dehydro-3-deoxy-galactarate (DDG) aldolase from Escherichia coli, in the presence and absence of substrate. The crystal structure was determined by locating only four Se sites to obtain phases for 506 protein residues. The protomer displays a modified (alpha/beta)(8) barrel fold, in which the eighth alpha-helix points away from the beta-barrel instead of packing against it. Analysis of the DDG aldolase crystal structures suggests a novel aldolase mechanism in which a phosphate anion accepts the proton from the methyl group of pyruvate.
==About this Structure==
==About this Structure==
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1DXF 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 MG and PYR as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-dehydro-3-deoxyglucarate_aldolase 2-dehydro-3-deoxyglucarate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.20 4.1.2.20] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DXF OCA].
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1DXF 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=MG:'>MG</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-dehydro-3-deoxyglucarate_aldolase 2-dehydro-3-deoxyglucarate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.20 4.1.2.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DXF OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blackwell, N.C.]]
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[[Category: Blackwell, N C.]]
[[Category: Izard, T.]]
[[Category: Izard, T.]]
[[Category: MG]]
[[Category: MG]]
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[[Category: class ii aldolase]]
[[Category: class ii aldolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:39:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:31 2008''

Revision as of 10:21, 21 February 2008


1dxf, resolution 2.6Å

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2-DEHYDRO-3-DEOXY-GALACTARATE ALDOLASE FROM ESCHERICHIA COLI IN COMPLEX WITH PYRUVATE

Overview

Carbon-carbon bond formation is an essential reaction in organic chemistry and the use of aldolase enzymes for the stereochemical control of such reactions is an attractive alternative to conventional chemical methods. Here we describe the crystal structures of a novel class II enzyme, 2-dehydro-3-deoxy-galactarate (DDG) aldolase from Escherichia coli, in the presence and absence of substrate. The crystal structure was determined by locating only four Se sites to obtain phases for 506 protein residues. The protomer displays a modified (alpha/beta)(8) barrel fold, in which the eighth alpha-helix points away from the beta-barrel instead of packing against it. Analysis of the DDG aldolase crystal structures suggests a novel aldolase mechanism in which a phosphate anion accepts the proton from the methyl group of pyruvate.

About this Structure

1DXF is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as 2-dehydro-3-deoxyglucarate aldolase, with EC number 4.1.2.20 Full crystallographic information is available from OCA.

Reference

Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism., Izard T, Blackwell NC, EMBO J. 2000 Aug 1;19(15):3849-56. PMID:10921867

Page seeded by OCA on Thu Feb 21 12:21:31 2008

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