view article

Figure 6
(a) Configuration of SFG, GPP and Mg2+ in the active site as a stereoview. Coordination of Tyr59 and Glu181 around the GPP C2 atom as well as Tyr59, Tyr185 and Phe230 facing the GPP C3 atom are also shown. The C2 and C3 atoms are labelled. The numbers next to dotted lines indicate the distance between atoms. The same colouring is used as in Fig. 4[link](e). (b) Conserved bicarbonate ion and Glu residue in the active sites of GPPMT (substrate-bound form), CmaA1 (PDB entry1kph ), CmaA2 (PDB entry 1kpi ), PcaA (PDB entry 1l1e ; Huang et al., 2002BB15) and Hma (PDB entry 2fk8 ; Boissier et al., 2006BB3). All proteins are shown as grey cartoons. C atoms of SFG, GPP and Glu181 of the substrate-bound GPPMT is shown in magenta. C atoms of SAH, didecyldimethylammonium bromide (DDDMAB) and the bicarbonate ion of CmaA1 are shown in light blue. C atoms of SAH, DDDMAB and the bicarbonate ion of CmaA2 are shown in yellow. The C atom of SAH and the bicarbonate ion of PcaA are shown in green. The C atoms of SAM and Glu146 of Hma are shown in orange.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds