None of this seems particularly surprising to someone who was an undergraduate level of biochemistry knowledge. Thirty years ago the professor in my Proteins class made a few relevant important points in his lectures:
1) Only handful of amino acids in a enzyme structures were highly conserved. (Out of hundreds, generally less than ten.)
2) Those were generally in the reaction center.
3) Almost all single sequence replacements had no measurable effect on protein structure and function.
4) Across species the "same" protein can diverge in sequence by up to 40%, while keeping the same structure. Sometimes this goes as far as 80%.
Given these basic facts, the findings in the paper aren't really surprising to anyone who studies proteins.
[Note: As with everything in biology, you can find counter examples. The histone proteins involved in DNA packing have an incredibly conserved sequence.]
1) Only handful of amino acids in a enzyme structures were highly conserved. (Out of hundreds, generally less than ten.)
2) Those were generally in the reaction center.
3) Almost all single sequence replacements had no measurable effect on protein structure and function.
4) Across species the "same" protein can diverge in sequence by up to 40%, while keeping the same structure. Sometimes this goes as far as 80%.
Given these basic facts, the findings in the paper aren't really surprising to anyone who studies proteins.
[Note: As with everything in biology, you can find counter examples. The histone proteins involved in DNA packing have an incredibly conserved sequence.]