5kf6

Structure of proline utilization A from Sinorhizobium meliloti complexed with L-tetrahydrofuroic acid and NAD+ in space group P21

spinqualitylabelsall models 5kf6, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5kf6 is a 2 chain structure with sequence from Sinmm. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, MG, NAD, PG4, PGE, TFB Related: 5kf7 Gene: putA, SM11_chr0102 (SINMM) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [F7X6I3_SINMM] Oxidizes proline to glutamate for use as a carbon and nitrogen source.[PIRNR:PIRNR000197] Publication Abstract from PubMed Aldehyde dehydrogenases (ALDHs) catalyze the NAD(P)+-dependent oxidation of aldehydes to carboxylic acids and are important for metabolism and detoxification. Although the ALDH superfamily fold is well established, some ALDHs contain an uncharacterized domain of unknown function (DUF) near the C-terminus of the polypeptide chain. Herein, we report the first structure of a protein containing the ALDH superfamily DUF. Proline utilization A from Sinorhizobium meliloti (SmPutA) is a 1233-residue bifunctional enzyme that contains the DUF in addition to proline dehydrogenase and L-glutamate-gamma-semialdehyde dehydrogenase catalytic modules. Structures of SmPutA with a proline analog bound to the proline dehydrogenase site and NAD+ bound to the ALDH site were determined in two space groups at 1.7 - 1.9 A resolution. The DUF consists of a Rossmann dinucleotide-binding fold fused to a 3-stranded beta-flap. The Rossmann domain resembles the classic ALDH superfamily NAD+-binding domain, while the flap is strikingly similar to the ALDH superfamily dimerization domain. Paradoxically, neither structural element performs its implied function. Electron density maps show that NAD+ does not bind to the DUF Rossmann fold. And small-angle X-ray scattering reveals a novel dimer that has never been seen in the ALDH superfamily. The structure suggests that the DUF is an adapter domain that stabilizes the aldehyde substrate binding loop and seals the substrate-channeling tunnel via tertiary structural interactions that mimic the quaternary structural interactions found in non-DUF PutAs. Kinetic data for SmPutA indicate a substrate-channeling mechanism, in agreement with previous studies of other PutAs. Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function.,Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ J Biol Chem. 2016 Sep 27. pii: jbc.M116.756965. PMID:27679491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Proline utilization A

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