6ags

Structural insights for non-natural cofactor binding by the L310R/Q401C mutant of malic enzyme from Escherichia coli

spinqualitylabelsall models 6ags, resolution 2.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ags is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.31Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAO1_ECOLI Publication Abstract from PubMed The use of nicotinamide cytosine dinucleotide (NCD), a biocompatible nicotinamide adenosine dinucleotide (NAD) analogue, is of great scientific and biotechnological interest. Several redox enzymes have been devised to favor NCD, and have been successfully applied in creating NCD-dependent redox systems. However, molecular interactions between cofactor and protein have still to be disclosed in order to guide further engineering efforts. Here we report the structural analysis of an NCD-favoring malic enzyme (ME) variant derived from Escherichia coli. The X-ray crystal structure data revealed that the residues located at position 346 and 401 in ME acted as the "gatekeepers" of the adenine moiety binding cavity. When Arg346 was substituted with either acidic or aromatic residues, the corresponding mutants showed substantially reduced NCD preference. Inspired by these observations, we generated Lactobacillus helveticus derived d-lactate dehydrogenase variants at Ile177, the counterpart to Arg346 in ME, and found a similar trend in terms of cofactor preference changes. As many NAD-dependent oxidoreductases share key structural features, our results provide guidance for protein engineering to obtain more NCD-favoring variants. Structural Insights into Malic Enzyme Variants Favoring an Unnatural Redox Cofactor.,Liu Y, Guo X, Liu W, Wang J, Kent Zhao Z Chembiochem. 2021 May 14;22(10):1765-1768. doi: 10.1002/cbic.202000800. Epub 2021, Mar 18. PMID:33523590 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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