5u0m

Fatty aldehyde dehydrogenase from Marinobacter aquaeolei VT8 and cofactor complex

spinqualitylabelsall models 5u0m, resolution 3.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u0m is a 2 chain structure with sequence from Marinobacter nauticus VT8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.075Å Ligands: CIT, EDO, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ASTD_MARN8 Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.[HAMAP-Rule:MF_01174] Publication Abstract from PubMed Enzymes involved in lipid biosynthesis and metabolism play an important role in energy conversion and storage, and in the function of structural components such as cell membranes. The fatty aldehyde dehydrogenase (FAldDH) plays a central function in the metabolism of lipid intermediates, oxidizing fatty aldehydes to the corresponding fatty acid, and competing with pathways that would further reduce the fatty aldehydes to fatty alcohols or require the fatty aldehydes to produce alkanes. In this report, the genes for four putative FAldDH enzymes from Marinobacter aquaeolei VT8 and an additional enzyme from Acinetobacter baylyi were heterologously expressed in Escherichia coli and shown to display FAldDH activity. Five enzymes (Maqu_0438, Maqu_3316, Maqu_3410, Maqu_3572 and WP_004927398) were found to act on aldehydes ranging from acetaldehyde to hexadecanal, and also acted on the unsaturated long-chain palmitoleyl and oleyl aldehydes. A comparison of the specificity of these enzymes with various aldehydes is presented. Crystallization trials yielded diffraction quality crystals of one particular FAldDH (Maqu_3316) from M. aquaeolei VT8. Crystals were independently treated with both the NAD+ cofactor and the aldehyde substrate decanal, revealing specific details of the likely substrate binding pocket for this class of enzymes. A likely model for how the catalysis by the enzyme is accomplished is also provided.Importance: This study provides a comparison of multiple enzymes with the ability to oxidize fatty aldehydes to fatty acids, and provides a likely picture of how the fatty aldehyde and NAD+ is bound to the enzyme to facilitate catalysis. Based on the information obtained from this structural analysis and the comparisons of specificity for the five enzymes that were characterized, correlations may be drawn to the potential roles played by specific residues within the structure. Characterization of five fatty aldehyde dehydrogenase enzymes from Marinobacter and Acinetobacter: structural insights into the aldehyde binding pocket.,Bertram JH, Mulliner KM, Shi K, Plunkett MH, Nixon P, Serratore NA, Douglas CJ, Aihara H, Barney BM Appl Environ Microbiol. 2017 Apr 7. pii: AEM.00018-17. doi: 10.1128/AEM.00018-17. PMID:28389542 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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