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| | {{STRUCTURE_1jq5| PDB=1jq5 | SCENE= }} | | {{STRUCTURE_1jq5| PDB=1jq5 | SCENE= }} |
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| - | '''Bacillus Stearothermophilus Glycerol dehydrogenase complex with NAD+'''
| + | ===Bacillus Stearothermophilus Glycerol dehydrogenase complex with NAD+=== |
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| - | ==Overview==
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| - | BACKGROUND: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD(+) 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD(+) to NADH. Analysis of the sequence of this enzyme indicates that it is a member of the so-called iron-containing alcohol dehydrogenase family. Despite this sequence similarity, GlyDH shows a strict dependence on zinc for activity. On the basis of this, we propose to rename this group the family III metal-dependent polyol dehydrogenases. To date, no structural data have been reported for any enzyme in this group. RESULTS: The crystal structure of B. stearothermophilus glycerol dehydrogenase has been determined at 1.7 A resolution to provide structural insights into the mechanistic features of this family. The enzyme has 370 amino acid residues, has a molecular mass of 39.5 kDa, and is a homooctamer in solution. CONCLUSIONS: Analysis of the crystal structures of the free enzyme and of the binary complexes with NAD(+) and glycerol show that the active site of GlyDH lies in the cleft between the enzyme's two domains, with the catalytic zinc ion playing a role in stabilizing an alkoxide intermediate. In addition, the specificity of this enzyme for a range of diols can be understood, as both hydroxyls of the glycerol form ligands to the enzyme-bound Zn(2+) ion at the active site. The structure further reveals a previously unsuspected similarity to dehydroquinate synthase, an enzyme whose more complex chemistry shares a common chemical step with that catalyzed by glycerol dehydrogenase, providing a striking example of divergent evolution. Finally, the structure suggests that the NAD(+) binding domain of GlyDH may be related to that of the classical Rossmann fold by switching the sequence order of the two mononucleotide binding folds that make up this domain.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11566129}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11566129 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11566129}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nad]] | | [[Category: Nad]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:36:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:37:39 2008'' |
Revision as of 17:37, 1 July 2008
Template:STRUCTURE 1jq5
Bacillus Stearothermophilus Glycerol dehydrogenase complex with NAD+
Template:ABSTRACT PUBMED 11566129
About this Structure
1JQ5 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Glycerol dehydrogenase. structure, specificity, and mechanism of a family III polyol dehydrogenase., Ruzheinikov SN, Burke J, Sedelnikova S, Baker PJ, Taylor R, Bullough PA, Muir NM, Gore MG, Rice DW, Structure. 2001 Sep;9(9):789-802. PMID:11566129
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