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PDBsum entry 1php
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References listed in PDB file
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Key reference
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Title
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Structure of the ADP complex of the 3-Phosphoglycerate kinase from bacillus stearothermophilus at 1.65 a.
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Authors
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G.J.Davies,
S.J.Gamblin,
J.A.Littlechild,
Z.Dauter,
K.S.Wilson,
H.C.Watson.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1994,
50,
202-209.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the ADP complex of the enzyme 3-phosphoglycerate kinase (PGK,
E.C. 2.7.2.3) from Bacillus stearothermophilus NCA-1503 has been determined by
the method of molecular replacement. The structure has been refined to an R
factor of 0.16 for all data between 10.0 and 1.65 A resolution, using data
collected on the Hendrix-Lentfer imaging plate at the EMBL outstation in
Hamburg. The r.m.s. deviations from stereochemical ideality are 0.010 and 0.011
A for bonds and planes, respectively. Although crystallized in the presence of
the nucleotide product MgATP, the high-resolution structure reveals the bound
nucleotide to be MgADP reflecting the low intrinsic ATPase activity of PGK.
Although the two domains of this enzyme are found to be some 4.5 degrees closer
together than is found in the yeast and horse-muscle apo-enzyme structures, this
structure represents the 'open' rather than the 'closed', catalytically
competent form, of the enzyme.
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Figure 1.
Fig. 1. Ribbon diagram, drawn with the MOLSCRIPTprogram (Kraulis,
1990), howing the structure of B. stearothermophilus PGK. The nu-
cleotide substrate atos are shown in 'ball-and-stck' representatin.
Te 3-PGA site, on the N-terminal domain, as detemined by Harlos,
Vas & Blake (1992) for the pig-muscle enzyme, is indicated.
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Figure 9.
Fig. 9. Schematic diagram illustratig the main interactions of the
nucleotide substrate, ADP, with the enzyme.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1994,
50,
202-209)
copyright 1994.
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Secondary reference #1
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Title
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The structure of a thermally stable 3-Phosphoglycerate kinase and a comparison with its mesophilic equivalent.
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Authors
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G.J.Davies,
S.J.Gamblin,
J.A.Littlechild,
H.C.Watson.
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Ref.
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Proteins, 1993,
15,
283-289.
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PubMed id
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Secondary reference #2
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Title
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Purification, Crystallisation and preliminary X-Ray analysis of the 3-Phosphoglycerate kinase from bacillus stearothermophilus
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Authors
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G.J.Davies,
S.J.Gamblin,
J.A.Littlechild,
H.C.Watson.
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Ref.
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j mol biol, 1992,
227,
1263.
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Secondary reference #3
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Title
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Sequence and expression of the gene encoding 3-Phosphoglycerate kinase from bacillus stearothermophilus.
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Authors
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G.J.Davies,
J.A.Littlechild,
H.C.Watson,
L.Hall.
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Ref.
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Gene, 1991,
109,
39-45.
[DOI no: ]
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PubMed id
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