Crystal structures and kinetic studies of a laboratory evolved aldehyde reductase explain the dramatic shift of its new substrate specificity

Sridhar, S.; Zavarise, A.; Kiema, T.-R.; Dalwani, S.; Eriksson, T.; Hajee, Y.; Reddy Enugala, T.; Wierenga, R.K.; Widersten, M.

doi:10.1107/S205225252300444X

Figure 3
The two amino acid substitutions of the DA1472 variant make the substrate specificity pocket wider. In this figure, the mode of binding of NADH (magenta sticks) and Fe²⁺ to the active site of the DA1472 variant are shown, as well as (in yellow) the residues Gly151 and Val259 (PDB entry 7qnh). Also shown are the superimposed NAD⁺ (gray sticks), as well as the residues Asn151 (orange, from the NAD-binding domain) and Leu259 (green, from the Fe²⁺-binding domain) of the wild-type active site (PDB entry 5br4). The mode of binding of the product of the reduction reaction, ethyleneglycol (EDO, cyan), which interacts with its oxygen atom with the Fe²⁺ ion (PDB entry 7qnf), as highlighted by a dotted line. `H' identifies the N-terminal end of the pyrophosphate-binding helix of the NAD-binding domain (brown).

IUCrJ

Volume 10| Part 4| July 2023| Pages 437-447

ISSN: 2052-2525

https://doi.org/10.1107/S205225252300444X

BIOLOGY | MEDICINE

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