view article
Figure 5
Conservation of amino-acid residues of Tah1. (a) Sequence alignment showing conserved residues in Tah1 sequences. Position 81 is indicated. TETPH, Tetrapisispora phaffii; KLUMA, Kluyveromyces marxianus; NAUCC, Naumovozyma castellii; SACCE, Saccharomyces cerevisiae; SACAR, Saccharomyces arboricola. Asterisks and dots below the alignment signify the degree of conservation. (b) Monomeric Tah1 showing the solvent-exposed position of Gln81. M represents the methionine residue of the MEEVD peptide. (c) Dimeric Tah1 showing the interactions made by the Gln81 residues of Tah1. M represents the methionine residue of the MEEVD peptide.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 71| Part 5| May 2015| Pages 1197-1206
https://doi.org/10.1107/S1399004715004551
Follow Acta Cryst. D
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS