7eth

Crystal structure of AbHpaI-Zn-pyruvate-propionaldehyde complex, Class II aldolase, HpaI from Acinetobacter baumanniiCrystal structure of AbHpaI-Zn-pyruvate-propionaldehyde complex, Class II aldolase, HpaI from Acinetobacter baumannii

Structural highlights 7eth is a 3 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A8I1ZEE8_ACIBA Publication Abstract from PubMed Aldolases catalyze the reversible reactions of aldol condensation and cleavage and have strong potential for the synthesis of chiral compounds, widely used in pharmaceuticals. Here, we investigated a new Class II metal aldolase from the p-hydroxyphenylacetate degradation pathway in Acinetobacter baumannii, 4-hydroxy-2-keto-heptane-1,7-dioate aldolase (AbHpaI), which has various properties suitable for biocatalysis, including stereoselectivity/stereospecificity, broad aldehyde utilization, thermostability, and solvent tolerance. Notably, the use of Zn(2+) by AbHpaI as a native cofactor is distinct from other enzymes in this class. AbHpaI can also use other metal ion (M(2+)) cofactors, except Ca(2+), for catalysis. We found that Zn(2+) yielded the highest enzyme complex thermostability (Tm of 87 degrees C) and solvent tolerance. All AbHpaI*M(2+) complexes demonstrated preferential cleavage of (4R)-2-keto-3-deoxy-D-galactonate ((4R)-KDGal) over (4S)-2-keto-3-deoxy-D-gluconate ((4S)-KDGlu), with AbHpaI*Zn(2+) displaying the highest R/S stereoselectivity ratio (sixfold higher than other M(2+) cofactors). For the aldol condensation reaction, AbHpaI*M(2+) only specifically forms (4R)-KDGal and not (4S)-KDGlu and preferentially catalyzes condensation rather than cleavage by approximately 40-fold. Based on 11 X-ray structures of AbHpaI complexed with M(2+) and ligands at 1.85 to 2.0 A resolution, the data clearly indicate that the M(2+) cofactors form an octahedral geometry with Glu151 and Asp177, pyruvate, and water molecules. Moreover, Arg72 in the Zn(2+)-bound form governs the stereoselectivity/stereospecificity of AbHpaI. X-ray structures also show that Ca(2+) binds at the trimer interface via interaction with Asp51. Hence, we conclude that AbHpaI*Zn(2+) is distinctive from its homologues in substrate stereospecificity, preference for aldol formation over cleavage, and protein robustness, and is attractive for biocatalytic applications. Catalytic and structural insights into a stereospecific and thermostable Class II aldolase HpaI from Acinetobacter baumannii.,Watthaisong P, Binlaeh A, Jaruwat A, Lawan N, Tantipisit J, Jaroensuk J, Chuaboon L, Phonbuppha J, Tinikul R, Chaiyen P, Chitnumsub P, Maenpuen S J Biol Chem. 2021 Oct 5;297(5):101280. doi: 10.1016/j.jbc.2021.101280. PMID:34624314 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase 3D structures

spinqualitylabelsall models 7eth, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image