1b14: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
|SITE= <scene name='pdbsite=ACA:Catalytic+Triad'>ACA</scene>, <scene name='pdbsite=ACB:Catalytic+Triad'>ACB</scene>, <scene name='pdbsite=CAA:Ca2++Binding+Residues'>CAA</scene>, <scene name='pdbsite=CAB:Ca2++Binding+Residues'>CAB</scene>, <scene name='pdbsite=NA1:Nad+Binding+Motif+In+Dadhs+G(A)Xgxxg'>NA1</scene>, <scene name='pdbsite=NA2:Nad+Binding+Motif+In+Sdrs+Gxxxgxg'>NA2</scene>, <scene name='pdbsite=NA3:Nad/Nadp+Selectivity+Amino+Acid'>NA3</scene>, <scene name='pdbsite=NB1:Nad+Binding+Motif+In+Dadhs+G(A)Xgxxg'>NB1</scene>, <scene name='pdbsite=NB2:Nad+Binding+Motif+In+Sdrs+Gxxxgxg'>NB2</scene> and <scene name='pdbsite=NB3:Nad/Nadp+Selectivity+Amino+Acid'>NB3</scene> | |SITE= <scene name='pdbsite=ACA:Catalytic+Triad'>ACA</scene>, <scene name='pdbsite=ACB:Catalytic+Triad'>ACB</scene>, <scene name='pdbsite=CAA:Ca2++Binding+Residues'>CAA</scene>, <scene name='pdbsite=CAB:Ca2++Binding+Residues'>CAB</scene>, <scene name='pdbsite=NA1:Nad+Binding+Motif+In+Dadhs+G(A)Xgxxg'>NA1</scene>, <scene name='pdbsite=NA2:Nad+Binding+Motif+In+Sdrs+Gxxxgxg'>NA2</scene>, <scene name='pdbsite=NA3:Nad/Nadp+Selectivity+Amino+Acid'>NA3</scene>, <scene name='pdbsite=NB1:Nad+Binding+Motif+In+Dadhs+G(A)Xgxxg'>NB1</scene>, <scene name='pdbsite=NB2:Nad+Binding+Motif+In+Sdrs+Gxxxgxg'>NB2</scene> and <scene name='pdbsite=NB3:Nad/Nadp+Selectivity+Amino+Acid'>NB3</scene> | ||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1b15|1B15]], [[1b2l|1B2L]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b14 OCA], [http://www.ebi.ac.uk/pdbsum/1b14 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b14 RCSB]</span> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Gonzalez-Duarte, R.]] | [[Category: Gonzalez-Duarte, R.]] | ||
[[Category: Ladenstein, R.]] | [[Category: Ladenstein, R.]] | ||
[[Category: alcohol dehydrogenase]] | [[Category: alcohol dehydrogenase]] | ||
[[Category: binary complex]] | [[Category: binary complex]] | ||
| Line 35: | Line 37: | ||
[[Category: short-chain dehydrogenases/reductase]] | [[Category: short-chain dehydrogenases/reductase]] | ||
''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 18:51:35 2008'' | ||
Revision as of 18:51, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , , and | ||||||
| Ligands: | |||||||
| Activity: | Alcohol dehydrogenase, with EC number 1.1.1.1 | ||||||
| Related: | 1B15, 1B2L
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALCOHOL DEHYDROGENASE FROM DROSOPHILA LEBANONENSIS BINARY COMPLEX WITH NAD+
OverviewOverview
Drosophila alcohol dehydrogenase (DADH; EC 1.1.1.1) is a NAD(H)-dependent oxidoreductase belonging to the short-chain dehydrogenases/reductases (SDR) family. This homodimeric enzyme catalyzes the dehydrogenation of alcohols to their respective ketones or aldehydes in the fruit-fly Drosophila, both for metabolic assimilation and detoxification purposes. The crystal structure of the apo form of DADH, one of the first biochemically characterized member of the SDR family, was solved at 1.9 A resolution by Patterson methods. The initial model was improved by crystallographic refinement accompanied by electron density averaging, R-factor=20.5%, R-free=23.8%.DADH subunits show an alpha/beta single domain structure with a characteristic NAD(H) binding motif (Rossmann fold). The peptide chain of a subunit is folded into a central eight-stranded beta-sheet flanked on each side by three alpha-helices. The dimers have local 2-fold symmetry. Dimer association is dominated by a four-helix bundle motif as well as two C-terminal loops from each subunit, which represent a unique structural feature in SDR enzymes with known structure.Three structural features are characteristic for the active site architecture. (1) A deep cavity which is covered by a flexible loop (33 residues) and the C-terminal tail (11 residues) from the neighboring subunit. The hydrophobic surface of the cavity is likely to increase the specificity of this enzyme towards secondary aliphatic alcohols. (2) The residues of the catalytic triad (Ser138, Tyr151, Lys155) are known to be involved in enzymatic catalysis in the first line. The Tyr151 OH group is involved in an ionic bond with the Lys155 side-chain. Preliminary electrostatic calculations have provided evidence that the active form of Tyr151 is a tyrosinate ion at physiological pH. (3) Three well-ordered water molecules in hydrogen bond distance to side-chains of the catalytic triad may be significant for the proton release steps in DADH catalysis.A ternary structure-based sequence alignment with ten members of the SDR family with known three-dimensional structure has suggested to define a model consisting of four groups of residues, which relates the observed low degree of sequence identity to quite similar folding patterns and nearly identical distributions of residues involved in catalysis.
About this StructureAbout this Structure
1B14 is a Single protein structure of sequence from Scaptodrosophila lebanonensis. Full crystallographic information is available from OCA.
ReferenceReference
The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution., Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R, J Mol Biol. 1998 Sep 18;282(2):383-99. PMID:9735295
Page seeded by OCA on Sun Mar 30 18:51:35 2008