Evolution of a new enzyme activity from the same motif fold.

Molecular Microbiology
Petr G Leiman, Ian J Molineux

Abstract

The host cell recognition protein of the Escherichia coli bacteriophage HK620 is a large homotrimeric tailspike that cleaves the O18A1 type O antigen. The crystal structure of HK620 tailspike determined in the apo and substrate-bound form is reported by Barbirz et al. in this issue of Molecular Microbiology. Lacking detectable sequence similarity, the fold and overall organization of the HK620 tailspike are similar to those of the tailspikes of the related phages P22 and Sf6. The substrate-binding site is intrasubunit in P22 and HK620 tailspikes, but intersubunit in Sf6, demonstrating how phages can adapt the same protein fold to recognize different substrates.

References

Oct 1, 1996·Proceedings of the National Academy of Sciences of the United States of America·S SteinbacherR Huber
May 13, 2006·Molecular Microbiology·Katharina StummeyerMartina Mühlenhoff

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Citations

Feb 7, 2018·Molecular Microbiology·Nicholas M I TaylorPetr G Leiman
Nov 28, 2017·Scientific Reports·Tomasz OlszakZuzanna Drulis-Kawa
Sep 30, 2017·Proteins·Andriy KryshtafovychTorsten Schwede
Sep 3, 2011·Microbiology and Molecular Biology Reviews : MMBR·David Veesler, Christian Cambillau
Jun 23, 2012·The Analyst·Amit SinghStephane Evoy
Mar 25, 2017·Applied Microbiology and Biotechnology·Agnieszka LatkaZuzanna Drulis-Kawa
Dec 6, 2019·Frontiers in Microbiology·Agnieszka LatkaYves Briers
Nov 9, 2018·Frontiers in Microbiology·Grazyna Majkowska-SkrobekZuzanna Drulis-Kawa
Jan 31, 2020·Frontiers in Microbiology·Leandra E KnechtLars Fieseler
Dec 7, 2010·Virology Journal·Petr G LeimanMichael G Rossmann

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