view article

Figure 1
(a) ClustalW alignment of PII paralogue protein sequences, numbered relative to the N. meningitidis PII sequence, with the T-loop (amino acids 37–55), B-loop (amino acids 81–90) and C-loop (amino acids 96–112) marked. The alignment view was generated with JALVIEW, with colouring according to the Zappo colour scheme, but applied only to residues showing a population identity of ≥80%. (b) `New-cartoon' format Cα-trace overlay of N. meningitidis PII and five other selected PII paralogue structures, illustrating tight conservation of the core region and the location of the B-, C- and T-loops relative to the ATP-binding cleft. N. meningitidis PII, PDB code 2gw8 , green; E. coli PII/GlnB, PDB code 2pii , red; E. coli GlnK, PDB code 2gnk , orange; H. seropedicae GlnK, PDB 1hwu , yellow; Synechococcus sp. GlnB, PDB code 1qy7 , purple; T. thermophilus TT021, PDB code 1v9o , dark blue. (c) `New-cartoon' format Cα trace of N. meningitidis PII coloured by chain showing a close-up view of the ATP-binding site, with conserved residues labelled according to the standard single-letter sequence code and displayed in `liquorice' format coloured purple. ATP is also shown in `liquorice' format coloured by name; the coordinates were derived from a Cα-trace overlay of E. coli ATP-bound structure PDB code 2gnk and N. meningitidis PII. (d) Cutaway view `new-cartoon' format Cα-trace of N. meningitidis PII coloured by chain, with selected residues labelled according to the standard single-letter sequence code and displayed in `liquorice' format and coloured by name, illustrating the central Lys60/Glu62 oligomerization contact and the conserved hydrophobic pocket. ATP is also shown in `liquorice' format coloured orange, with coordinates derived from a Cα-trace overlay of E. coli ATP-bound structure PDB code 2gnk and N. meningitidis PII.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds