view article

Figure 2
Comparative analysis of Rv3717 with other N-acetylmuramoyl-L-alanine amidases. (a) Stereoview of the superposition of rRv3717-B (magenta) with representative EADs of N-acetylmuramoyl-L-alanine amidases from Bartonella henselae (PDB entry 3ne8; cyan) or Bacillus polymxa (PDB entry 1jwq; green) indicates structural similarities (see text for more details). A bound zinc ion (sphere) marks the active site of Rv3717. The 16β-hairpin36 at the N-terminus and 148loop154 of Rv3717 (shown in blue) partially occlude the active site. Active-site residues in Rv3717 in coordination with Zn2+ are shown in stick representation. (b) Sequence alignment of Rv3717 and its structural homologues as identified from DALI. Sequences are shown in the same colours as their structural counterparts in (a).

Journal logoSTRUCTURAL
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds