Figure 4.
Fig. 4. Model to ATP and 2-oxoglutarate binding sites in
HsPII protein. (A ) Diagram of a C trace overlay
of HsPII (orange) with CHMI (cyan) [31]. A top view of the
trimers similar in orientation to Figs 1A and 2Bii Go-. The
different views of the proposed 2-oxoglutarate and ATP-binding
sites in HsPII protein are shown in (B ), (C ) and (D). (B)
Position of ATP and 2-oxo-3-pentynoate in the lateral cleft of
HsPII. (C) ATP molecule and the neighbouring amino-acid
residues. (D ) 2-oxo-3-pentynoate molecule and the neighbour
amino-acid residues. Location of ATP and 2-oxo-3-pentynoate was
modelled using HsPII, EcGlnK-ATP, EcPII-ATP and 4-oxalocrotonate
tautomerase-2-oxo-3-pentynoate structures using dali and
lsqkab[8,14,15].
The above figure is reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2002,
269,
3296-3303)
copyright 2002.
trace overlay
of HsPII (orange) with CHMI (cyan) [31]. A top view of the
trimers similar in orientation to Figs 1A and 2Bii Go-
. The
different views of the proposed 2-oxoglutarate and ATP-binding
sites in HsPII protein are shown in (B ), (C ) and (D). (B)
Position of ATP and 2-oxo-3-pentynoate in the lateral cleft of
HsPII. (C) ATP molecule and the neighbouring amino-acid
residues. (D ) 2-oxo-3-pentynoate molecule and the neighbour
amino-acid residues. Location of ATP and 2-oxo-3-pentynoate was
modelled using HsPII, EcGlnK-ATP, EcPII-ATP and 4-oxalocrotonate
tautomerase-2-oxo-3-pentynoate structures using dali and
lsqkab[8,14,15].