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-Structure paper
タイトル | Substrate specificity of plant nitrilase complexes is affected by their helical twist. |
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ジャーナル・号・ページ | Commun Biol, Vol. 1, Page 186, Year 2018 |
掲載日 | 2018年11月2日 |
著者 | Jeremy D Woodward / Inga Trompetter / B Trevor Sewell / Markus Piotrowski / |
PubMed 要旨 | Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important ...Nitrilases are oligomeric, helix-forming enzymes from plants, fungi and bacteria that are involved in the metabolism of various natural and artificial nitriles. These biotechnologically important enzymes are often specific for certain substrates, but directed attempts at modifying their substrate specificities by exchanging binding pocket residues have been largely unsuccessful. Thus, the basis for their selectivity is still unknown. Here we show, based on work with two highly similar nitrilases from the plant , that modifying nitrilase helical twist, either by exchanging an interface residue or by imposing a different twist, without altering any binding pocket residues, changes substrate preference. We reveal that helical twist and substrate size correlate and when binding pocket residues are exchanged between two nitrilases that show the same twist but different specificities, their specificities change. Based on these findings we propose that helical twist influences the overall size of the binding pocket. |
リンク | Commun Biol / PubMed:30417123 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 20.0 Å |
構造データ | EMDB-3486: EMDB-3496: EMDB-3497: EMDB-3498: EMDB-3499: EMDB-3500: EMDB-3501: EMDB-3503: EMDB-3504: EMDB-3505: |
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