Yw. Liu et al., STRUCTURE OF RABBIT MUSCLE PHOSPHOGLUCOMUTASE REFINED AT 2.4 ANGSTROMRESOLUTION, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 392-405
Citations number
30
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
Data between 6.0 and 2.4 Angstrom resolution, collected at 253 K, were
used to refine a revised atomic model of muscle phosphoglucomutase: f
inal crystallographic R factor = 16.3% (R-free = 19.1%); final r.m.s.
deviations from ideal bond lengths and angles = 0.018 Angstrom and 3.2
degrees, respectively. Features of the protein that were recognized o
nly in the revised model include: the disposition of water molecules w
ithin domain-domain interfaces; two ion pairs buried in domain-domain
interfaces, one of which is a structural arginine around which the act
ive-site phosphoserine loop is wound; the basic architecture of the ac
tive-site 'crevice', which is a groove in a 1 1/3-turn helix, open at
both ends, that is produced by the interfacing of the four domains; th
e distorted hexacoordinate ligand sphere of the active-site Mg2+, wher
e the enzymic phosphate group acts as a bidentate ligand; a pair of ar
ginine residues in domain IV that form part of the enzymic phosphate-b
inding site (distal subsite) whose disposition in the two monomers of
the asymmetric unit is affected unequally by distant crystallographic
contacts; structural differences throughout domain IV, produced by the
se differing contacts, that may mimic solution differences induced by
substrate binding; large differences in individually refined Debye-Wal
ler thermal factors for corresponding main-chain atoms in monomers (1)
and (2), suggesting a dynamic disorder within the crystal that may in
volve domain-size groups of residues; and a 'nucleophilic elbow' in th
e active site that resides in a topological environment differing from
previous descriptions of this type of structure in other proteins.