3fpl

File:3fpl.png

spinqualitylabelsall models PDB ID 3fpl Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
3fpl, resolution 1.90Å ()
Ligands:	, , , ,
Gene:	ADH1, ADH1 ("Clostridium rubrum" Ng and Vaughn 1963)
Activity:	Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2
Related:	3fpc
Structural annotation: Resources: CATH : 3Fpla01, 3Fpla02 InterPro : Ipr002085, Ipr002328, Ipr011032, Ipr013149, Ipr013154 Pfam : PF00107, PF08240
Evolutionary conservation: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADHChimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH

Publication Abstract from PubMed

---

The cofactor-binding domains (residues 153-295) of the alcohol dehydrogenases from the thermophile Thermoanaerobacter brockii (TbADH), the mesophilic bacterium Clostridium beijerinckii (CbADH), and the protozoan parasite Entamoeba histolytica (EhADH1) have been exchanged. Three chimeras have been constructed. In the first chimera, the cofactor-binding domain of thermophilic TbADH was replaced with the cofactor-binding domain of its mesophilic counterpart CbADH [chimera Chi21((TCT))]. This domain exchange significantly destabilized the parent thermophilic enzyme (DeltaT(1/2) = -18 degrees C). The reverse exchange in CbADH [chimera Chi22((CTC))], however, had little effect on the thermal stability of the parent mesophilic protein. Furthermore, substituting the cofactor-binding domain of TbADH with the homologous domain of EhADH1 [chimera Chi23((TET))] substantially reduced the thermal stability of the thermophilic ADH (DeltaT(1/2) = -51 degrees C) and impeded the oligomerization of the enzyme. All three chimeric proteins and one of their site-directed mutants were crystallized, and their three-dimensional (3D) structures were determined. Comparison of the 3D structures of the chimeras and the chimeric mutant with the structures of their parent ADHs showed no significant changes to their Calpha chains, suggesting that the difference in the thermal stability of the three parent ADHs and their chimeric mutants could be due to a limited number of substitutions located at strategic positions, mainly at the oligomerization interfaces. Indeed, stabilization of the chimeras was achieved, to a significant extent, either by introduction of a proline residue at a strategic position in the major horse liver ADH-type dimerization interface (DeltaT(1/2) = 35 degrees C) or by introduction of intersubunit electrostatic interactions (DeltaT(1/2) = 6 degrees C).

Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms., Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y, Biochemistry. 2010 Feb 9. PMID:20102159

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

3fpl is a 1 chain structure of Alcohol dehydrogenase with sequence from Clostridium beijerinckii, thermoanaerobacter brockii. Full crystallographic information is available from OCA.

See AlsoSee Also

• Alcohol dehydrogenase
• Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH
• Chimeras of alcohol dehydrogenases
• Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH
• Tetrameric alcohol dehydrogenases