1eun

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[[Image:1eun.gif|left|200px]]
[[Image:1eun.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1eun |SIZE=350|CAPTION= <scene name='initialview01'>1eun</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1eun", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1eun| PDB=1eun | SCENE= }}
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|RELATEDENTRY=[[1eua|1EUA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eun OCA], [http://www.ebi.ac.uk/pdbsum/1eun PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eun RCSB]</span>
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}}
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'''STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE FROM ESCHERICHIA COLI'''
'''STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE FROM ESCHERICHIA COLI'''
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[[Category: Sygusch, J.]]
[[Category: Sygusch, J.]]
[[Category: 2-keto-3-deoxy-6-phosphogluconate aldolase]]
[[Category: 2-keto-3-deoxy-6-phosphogluconate aldolase]]
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[[Category: beta-barrel]]
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[[Category: Beta-barrel]]
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[[Category: sulfate]]
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[[Category: Sulfate]]
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[[Category: trimer]]
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[[Category: Trimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:32:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:09:52 2008''
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Revision as of 12:32, 2 May 2008

Template:STRUCTURE 1eun

STRUCTURE OF 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE 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

1EUN 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 Page seeded by OCA on Fri May 2 15:32:05 2008

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