1eua
From Proteopedia
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|PDB= 1eua |SIZE=350|CAPTION= <scene name='initialview01'>1eua</scene>, resolution 1.95Å | |PDB= 1eua |SIZE=350|CAPTION= <scene name='initialview01'>1eua</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eun|1EUN]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eua OCA], [http://www.ebi.ac.uk/pdbsum/1eua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eua RCSB]</span> | ||
}} | }} | ||
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[[Category: Grochulski, P.]] | [[Category: Grochulski, P.]] | ||
[[Category: Sygusch, J.]] | [[Category: Sygusch, J.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: PYR]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: carbinolamine]] | [[Category: carbinolamine]] | ||
[[Category: trimer]] | [[Category: trimer]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:09:42 2008'' |
Revision as of 17:09, 30 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 | ||||||
| Related: | 1EUN
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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