Pooja Asthana
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poojaasthana.bsky.social
Pooja Asthana
@poojaasthana.bsky.social
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Reposted by Pooja Asthana
chicalab.bsky.social
How do mutations far from an enzyme's active site influence catalysis? 🤔

Part 2: In collaboration with @fraserlab.bsky.social and @silviaosuna.bsky.social, we investigated this question using de novo Kemp eliminases, revealing effects of distal mutations on the catalytic cycle. 🧵 (1/6)
February 28, 2025 at 5:09 PM
Reposted by Pooja Asthana
fraserlab.com
Our latest work on tackling streptogramin resistance in collaboration with the Seiple lab is now up as a preprint. We (led by Pooja Asthana) targeted a resistance enzyme, VatD, with fragment-based drug discovery!

www.biorxiv.org/content/10.1...
An annotated molecular surface representation of the VatD trimer highlighting three fragment binding sites: the Active site (pink), the Acetyl-CoA (Ac-CoA) site (blue), and Accessory sites (yellow). Fragment-bound molecules are visualized as stick models at their respective binding locations, showing the spatial arrangement of the trimer interface.
February 3, 2025 at 4:58 PM