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PDBsum entry 1csc
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Oxo-acid-lyase
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PDB id
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1csc
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References listed in PDB file
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Key reference
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Title
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1.9-A structures of ternary complexes of citrate synthase with d- And l-Malate: mechanistic implications.
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Authors
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M.Karpusas,
D.Holland,
S.J.Remington.
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Ref.
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Biochemistry, 1991,
30,
6024-6031.
[DOI no: ]
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
94%.
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Abstract
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The structures of four isomorphous crystals of ternary complexes of chicken
heart citrate synthase with D- or L-malate and acetyl coenzyme A or
carboxymethyl coenzyme A have been determined by X-ray crystallography and fully
refined at 1.9-A resolution. The structures show that both L-malate and D-malate
bind in a very similar way in the presence of acetylCoA and that the enzyme
conformation is "closed". Hydrogen bond geometry is suggested to account for the
difference in binding constants of the two stereoisomers. The structures suggest
that steric hindrance can account for the observation that proton exchange of
acetyl coenzyme A with solvent is catalyzed by citrate synthase in the presence
of L-malate but not D-malate. The ternary complexes with malate reveal the mode
of binding of the substrate acetylCoA in the ground state. The carbonyl oxygen
of the acetyl group is hydrogen bonded to a water molecule and to histidine 274,
allowing unambiguous identification of the orientation of this group. The
structures support the hypothesis that carboxymethyl coenzyme A is a
transition-state analogue for the enolization step of the reaction (Bayer et
al., 1981) and additionally support proposed mechanisms for the condensation
reaction (Karpusas et al., 1990; Alter et al., 1990).
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Secondary reference #1
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Title
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Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and s-Acetonyl-Coenzyme a.
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Authors
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G.Wiegand,
S.Remington,
J.Deisenhofer,
R.Huber.
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Ref.
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J Mol Biol, 1984,
174,
205-219.
[DOI no: ]
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PubMed id
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Figure 2.
FIG. 2. The small omains of the closed form (C2) and the closed form (P4,2,2) are optimally
superimposed and shown in the stereo diagram. The conformations also differ substantially for internal
residues as ndicated specifically for some residues.
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The above figure is
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 a resolution.
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Authors
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S.Remington,
G.Wiegand,
R.Huber.
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Ref.
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J Mol Biol, 1982,
158,
111-152.
[DOI no: ]
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PubMed id
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Figure 1.
BVIE
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Figure 19.
FIG. 19. Stereo drawing of the citryl-thioether-CoA analogue ((XC%NPH6) difference Fourier map
superimposed on the monoclinic model. Contours are at +49 e. with negative contours dashed. The
Figure is discussd in the text.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #3
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Title
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Primary structure of porcine heart citrate synthase.
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Authors
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D.P.Bloxham,
D.C.Parmelee,
S.Kumar,
R.D.Wade,
L.H.Ericsson,
H.Neurath,
K.A.Walsh,
K.Titani.
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Ref.
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Proc Natl Acad Sci U S A, 1981,
78,
5381-5385.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Crystal structure analysis of the tetragonal crystal form are preliminary molecular model of pig-Heart citrate synthase.
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Authors
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G.Wiegand,
D.Kukla,
H.Scholze,
T.A.Jones,
R.Huber.
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Ref.
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Eur J Biochem, 1979,
93,
41-50.
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PubMed id
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