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1eua

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[[Image:1eua.gif|left|200px]]<br /><applet load="1eua" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eua.gif|left|200px]]
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caption="1eua, resolution 1.95&Aring;" />
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'''SCHIFF BASE INTERMEDIATE IN KDPG ALDOLASE FROM ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1eua |SIZE=350|CAPTION= <scene name='initialview01'>1eua</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14]
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|GENE=
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}}
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'''SCHIFF BASE INTERMEDIATE IN KDPG ALDOLASE FROM ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EUA 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=ACT:'>ACT</scene>, <scene name='pdbligand=SO4:'>SO4</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-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUA OCA].
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1EUA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EUA OCA].
==Reference==
==Reference==
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Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution., Allard J, Grochulski P, Sygusch J, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3679-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11274385 11274385]
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Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution., Allard J, Grochulski P, Sygusch J, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3679-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11274385 11274385]
[[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]]
[[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:00:22 2008''

Revision as of 09:00, 20 March 2008

Image:1eua.gif


PDB ID 1eua

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , and
Activity: 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14
Coordinates: save as pdb, mmCIF, xml



SCHIFF BASE INTERMEDIATE IN KDPG ALDOLASE FROM ESCHERICHIA COLI


Overview

2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. The enzyme is a class I aldolase whose reaction mechanism involves formation of Schiff base intermediates between Lys-133 and a keto substrate. A covalent adduct was trapped by flash freezing KDPG aldolase crystals soaked with 10 mM pyruvate in acidic conditions at pH 4.6. Structure determination to 1.95-A resolution showed that pyruvate had undergone nucleophilic attack with Lys-133, forming a protonated carbinolamine intermediate, a functional Schiff base precursor, which was stabilized by hydrogen bonding with active site residues. Carbinolamine interaction with Glu-45 indicates general base catalysis of several rate steps. Stereospecific addition is ensured by aromatic interaction of Phe-135 with the pyruvate methyl group. In the native structure, Lys-133 donates all of its hydrogen bonds, indicating the presence of an epsilon-ammonium salt group. Nucleophilic activation is postulated to occur by proton transfer in the monoprotonated zwitterionic pair (Glu-45/Lys-133). Formation of the zwitterionic pair requires prior side chain rearrangement by protonated Lys-133 to displace a water molecule, hydrogen bonded to the zwitterionic residues.

About this Structure

1EUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution., Allard J, Grochulski P, Sygusch J, Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3679-84. PMID:11274385

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