Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8648172 | Journal of Structural Biology | 2018 | 11 Pages |
Abstract
Analysis of the SrlD cofactor and substrate binding sites identified residues important for the formation of the complex with cofactor and substrate and in particular the role of Lys42 in selectivity towards the phospho-substrate. The comparison of SrlD backbone with the backbone of 302 short-chain dehydrogenases/reductases showed the conservation of the protein core and identified the variable parts. The SrlD sequence was compared with 500 S6PDH sequences selected by homology revealing that the C-terminal part is more conserved than the N-terminal, the consensus of the catalytic tetrad (Y[SN]AGXA) and a not previously described consensus for the NAD(H) binding.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Marco Salomone-Stagni, Joseph D. Bartho, Eeshan Kalita, Martin Rejzek, Robert A. Field, Dom Bellini, Martin A. Walsh, Stefano Benini,