1llu
From Proteopedia
(New page: 200px<br /><applet load="1llu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llu, resolution 2.30Å" /> '''THE TERNARY COMPLEX ...) |
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| - | [[Image:1llu.gif|left|200px]]<br /><applet load="1llu" size=" | + | [[Image:1llu.gif|left|200px]]<br /><applet load="1llu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1llu, resolution 2.30Å" /> | caption="1llu, resolution 2.30Å" /> | ||
'''THE TERNARY COMPLEX OF PSEUDOMONAS AERUGINOSA ALCOHOL DEHYDROGENASE WITH ITS COENZYME AND WEAK SUBSTRATE'''<br /> | '''THE TERNARY COMPLEX OF PSEUDOMONAS AERUGINOSA ALCOHOL DEHYDROGENASE WITH ITS COENZYME AND WEAK SUBSTRATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Pseudomonas aeruginosa alcohol dehydrogenase (PaADH; ADH, EC 1.1.1.1) | + | Pseudomonas aeruginosa alcohol dehydrogenase (PaADH; ADH, EC 1.1.1.1) catalyzes the reversible oxidation of primary and secondary alcohols to the corresponding aldehydes and ketones, using NAD as coenzyme. We crystallized the ternary complex of PaADH with its coenzyme and a substrate molecule and determined its structure at a resolution of 2.3 A, using the molecular replacement method. The PaADH tetramer comprises four identical chains of 342 amino acid residues each and obeys ~222-point symmetry. The PaADH monomer is structurally similar to alcohol dehydrogenase monomers from vertebrates, archaea, and bacteria. The stabilization of the ternary complex of PaADH, the coenzyme, and the poor substrate ethylene glycol (k(cat) = 4.5 sec(-1); Km > 200 mM) was due to the blocked exit of the coenzyme in the crystalline state, combined with a high (2.5 M) concentration of the substrate. The structure of the ternary complex presents the precise geometry of the Zn coordination complex, the proton-shuttling system, and the hydride transfer path. The ternary complex structure also suggests that the low efficiency of ethylene glycol as a substrate results from the presence of a second hydroxyl group in this molecule. |
==About this Structure== | ==About this Structure== | ||
| - | 1LLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN, NAD and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http:// | + | 1LLU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: proton relay system]] | [[Category: proton relay system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:08 2008'' |
Revision as of 11:46, 21 February 2008
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THE TERNARY COMPLEX OF PSEUDOMONAS AERUGINOSA ALCOHOL DEHYDROGENASE WITH ITS COENZYME AND WEAK SUBSTRATE
Overview
Pseudomonas aeruginosa alcohol dehydrogenase (PaADH; ADH, EC 1.1.1.1) catalyzes the reversible oxidation of primary and secondary alcohols to the corresponding aldehydes and ketones, using NAD as coenzyme. We crystallized the ternary complex of PaADH with its coenzyme and a substrate molecule and determined its structure at a resolution of 2.3 A, using the molecular replacement method. The PaADH tetramer comprises four identical chains of 342 amino acid residues each and obeys ~222-point symmetry. The PaADH monomer is structurally similar to alcohol dehydrogenase monomers from vertebrates, archaea, and bacteria. The stabilization of the ternary complex of PaADH, the coenzyme, and the poor substrate ethylene glycol (k(cat) = 4.5 sec(-1); Km > 200 mM) was due to the blocked exit of the coenzyme in the crystalline state, combined with a high (2.5 M) concentration of the substrate. The structure of the ternary complex presents the precise geometry of the Zn coordination complex, the proton-shuttling system, and the hydride transfer path. The ternary complex structure also suggests that the low efficiency of ethylene glycol as a substrate results from the presence of a second hydroxyl group in this molecule.
About this Structure
1LLU is a Single protein structure of sequence from Pseudomonas aeruginosa with , and as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
The ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycol., Levin I, Meiri G, Peretz M, Burstein Y, Frolow F, Protein Sci. 2004 Jun;13(6):1547-56. PMID:15152088
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