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PDBsum entry 1fea
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Oxidoreductase
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PDB id
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1fea
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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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Crithidia fasciculata trypanothione reductase at 1.70 a resolution
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Authors
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C.L.Strickland,
P.A.Karplus.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Overexpression of crithidia fasciculata trypanothione reductase and crystallization using a novel geometry.
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Authors
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C.L.Strickland,
R.Puchalski,
S.N.Savvides,
P.A.Karplus.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1995,
51,
337-341.
[DOI no: ]
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PubMed id
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Figure 2.
Fig. 2. Plug drop crystallization design. A 1 cm length of glass tubing
with an internal diameter of 4 mm was siliconized and then epoxyed
onto a 12 mm diameter glass coverslip. 40 lal of the protein solution
to be crystallized (in this case made by mixing 24 lal of 10 mg ml -l
TR stock with 16 lal of the reservoir against which the plug would be
equilibrated) was placed in the epoxied glass tubing. The unit was
placed into a well of a Linbro tissue-culture plate and surrounded
with 500 lal of reservoir solution, and then the well was sealed.
Although the Linbro plate is convenient, the plug-drop unit could be
placed in any sealed container.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Structure of trypanothione reductase from crithidia fasciculata at 2.6 a resolution; enzyme-Nadp interactions at 2.8 a resolution.
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Authors
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S.Bailey,
A.H.Fairlamb,
W.N.Hunter.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1994,
50,
139-154.
[DOI no: ]
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PubMed id
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Figure 7.
Fig. 7. A scheatic representation of FAD binding showing
hydrogen-bond interactions (dashed lines) between the co-factor
and the prtein.
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Figure 10.
Fg. 10. A schematic representation of the NADP binding showing
hydrogen-bonding interactions (dashed lines) formed between the
co-factor and the protein.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #3
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Title
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The structure of trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state.
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Authors
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C.B.Lantwin,
I.Schlichting,
W.Kabsch,
E.F.Pai,
R.L.Krauth-Siegel.
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Ref.
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Proteins, 1994,
18,
161-173.
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PubMed id
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Secondary reference #4
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Title
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Substrate interactions between trypanothione reductase and n1-Glutathionylspermidine disulphide at 0.28-Nm resolution.
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Authors
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S.Bailey,
K.Smith,
A.H.Fairlamb,
W.N.Hunter.
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Ref.
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Eur J Biochem, 1993,
213,
67-75.
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PubMed id
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Secondary reference #5
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Title
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X-Ray structure of trypanothione reductase from crithidia fasciculata at 2.4-A resolution.
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Authors
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J.Kuriyan,
X.P.Kong,
T.S.Krishna,
R.M.Sweet,
N.J.Murgolo,
H.Field,
A.Cerami,
G.B.Henderson.
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Ref.
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Proc Natl Acad Sci U S A, 1991,
88,
8764-8768.
[DOI no: ]
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PubMed id
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