Slightly misleading headline, as PET (polyethylene terephthalate) hydrolases were already known - see https://www.chm.bris.ac.uk/motm/PETase/PETaseh.htm This is a study of an archaeal enzyme (from the deep-sea) that can degrade both long-chain and short-chain polymers that is more efficient at 70 deg C than other enzymes. The details are that this is a feruloyl esterase with a conserved alpha/beta-hydrolase fold but…
"this is a feruloyl esterase with a conserved alpha/beta-hydrolase fold but with an additional flexible 'lid' domain that covers the active site" As educated as I think I am, it is always humbling to read a hacker news comment that I cannot understand. ELI5?
So I'll break it down:
- "feruloyl esterase" : an 'esterase' is an enzyme that makes or breaks ester bonds. In this case, 'feruloyl' which I've never heard of but apparently is some small molecule that is normally attached to a sugar. https://en.wikipedia.org/wiki/Feruloyl_esterase
- "conserved alpha/beta-hydrolase fold" : a structural pattern (fold) that is shared (conserved) between a set of structures. In other words, these enzymes all have roughly the same shape. https://www.cathdb.info/version/v4_3_0/superfamily/3.40.50.1...
- "additional flexible 'lid' domain that covers the active site" : a 'domain' is just a compact part of a protein, without going into too much detail. They are calling it a 'flexible lid' as the idea is that it moves out of the way to bind the substrate to the active site (where the reaction is carried out) and back again when fully bound.