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PDBsum entry 1rae
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of ctp-Ligated t state aspartate transcarbamoylase at 2.5 a resolution: implications for atcase mutants and the mechanism of negative cooperativity.
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Authors
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R.P.Kosman,
J.E.Gouaux,
W.N.Lipscomb.
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Ref.
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Proteins, 1993,
15,
147-176.
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PubMed id
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Abstract
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The X-ray crystal structure of CTP-ligated T state aspartate transcarbamoylase
has been refined to an R factor of 0.182 at 2.5 A resolution using the computer
program X-PLOR. The structure contains 81 sites for solvent and has rms
deviations from ideality in bond lengths and bond angles of 0.018 A and 3.722
degrees, respectively. The cytosine base of CTP interacts with the main chain
carbonyl oxygens of rTyr-89 and rIle-12, the main chain NH of rIle-12, and the
amino group of rLys-60. The ribose hydroxyls form polar contacts with the amino
group of rLys-60, a carboxylate oxygen of rAsp-19, and the main chain carbonyl
oxygen of rVal-9. The phosphate oxygens of CTP interact with the amino group of
rLys-94, the hydroxyl of rThr-82, and an imidazole nitrogen of rHis-20. Recent
mutagenesis experiments evaluated in parallel with the structure reported here
indicate that alterations in the hydrogen bonding environment of the side chain
of rAsn-111 may be responsible for the homotropic behavior of the pAR5 mutant of
ATCase. The location of the first seven residues of the regulatory chain has
been identified for the first time in a refined ATCase crystal structure, and
the proximity of this portion of the regulatory chain to the allosteric site
suggests a potential role for these residues in nucleotide binding to the
enzyme. Finally, a series of amino acid side chain rearrangements leading from
the R1 CTP allosteric to the R6 CTP allosteric site has been identified which
may constitute the molecular mechanism of distinct CTP binding sites on ATCase.
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Secondary reference #1
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Title
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Structural consequences of effector binding to the t state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- And ctp-Complexed enzymes at 2.6-A resolution.
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Authors
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R.C.Stevens,
J.E.Gouaux,
W.N.Lipscomb.
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Ref.
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Biochemistry, 1990,
29,
7691-7701.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Structural asymmetry in the ctp-Liganded form of aspartate carbamoyltransferase from escherichia coli.
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Authors
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K.H.Kim,
Z.X.Pan,
R.B.Honzatko,
H.M.Ke,
W.N.Lipscomb.
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Ref.
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J Mol Biol, 1987,
196,
853-875.
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PubMed id
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Secondary reference #3
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Title
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Location of amino acid alterations in mutants of aspartate transcarbamoylase: structural aspects of interallelic complementation.
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Authors
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H.K.Schachman,
C.D.Pauza,
M.Navre,
M.J.Karels,
L.Wu,
Y.R.Yang.
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Ref.
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Proc Natl Acad Sci U S A, 1984,
81,
115-119.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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Nucleotide sequence of the structural gene (pyrb) that encodes the catalytic polypeptide of aspartate transcarbamoylase of escherichia coli.
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Authors
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T.A.Hoover,
W.D.Roof,
K.F.Foltermann,
G.A.O'Donovan,
D.A.Bencini,
J.R.Wild.
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Ref.
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Proc Natl Acad Sci U S A, 1983,
80,
2462-2466.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from escherichia coli.
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Authors
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W.H.Konigsberg,
L.Henderson.
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Ref.
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Proc Natl Acad Sci U S A, 1983,
80,
2467-2471.
[DOI no: ]
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PubMed id
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