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Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore. / Urbaniak, Michael D.; Muskett, Frederick W.; Finucane, Michael D. et al.
In: Biochemistry, Vol. 41, No. 39, 01.10.2002, p. 11731-11739.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Urbaniak, MD, Muskett, FW, Finucane, MD, Caddick, S & Woolfson, DN 2002, 'Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore', Biochemistry, vol. 41, no. 39, pp. 11731-11739. https://doi.org/10.1021/bi0262146

APA

Urbaniak, M. D., Muskett, F. W., Finucane, M. D., Caddick, S., & Woolfson, D. N. (2002). Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore. Biochemistry, 41(39), 11731-11739. https://doi.org/10.1021/bi0262146

Vancouver

Urbaniak MD, Muskett FW, Finucane MD, Caddick S, Woolfson DN. Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore. Biochemistry. 2002 Oct 1;41(39):11731-11739. doi: 10.1021/bi0262146

Author

Urbaniak, Michael D. ; Muskett, Frederick W. ; Finucane, Michael D. et al. / Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore. In: Biochemistry. 2002 ; Vol. 41, No. 39. pp. 11731-11739.

Bibtex

@article{d6c2aa479a054d7084b3b50f4e901278,
title = "Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore",
abstract = "The natural complex Neocarzinostatin comprises a labile chromophore noncovalently bound to an 11.2 kDa protein. We present the first high-resolution structure of a novel complex derived from the recombinant apoprotein bound to a non-natural synthetic chromophore. Fluorescence and nuclear magnetic resonance spectroscopy were used to probe the strength and location of binding. Binding occurred in a location similar to that observed for the chromophore in the natural Neocarzinostatin complex, but with a distinct orientation. These results provide structural evidence that the apoprotein can readily accommodate small druglike entities, other than the natural chromophore within its binding cleft. The clinical use of the natural complex described by others, together with the results reported here, suggests potential applications for small molecule binding by apo-Neocarzinostatin.",
keywords = "Antibiotics, Antineoplastic, Apoproteins, Binding Sites, Circular Dichroism, Crystallography, X-Ray, Enediynes, Nuclear Magnetic Resonance, Biomolecular, Recombinant Fusion Proteins, Solutions, Spectrometry, Fluorescence, Zinostatin",
author = "Urbaniak, {Michael D.} and Muskett, {Frederick W.} and Finucane, {Michael D.} and Stephen Caddick and Woolfson, {Derek N.}",
year = "2002",
month = oct,
day = "1",
doi = "10.1021/bi0262146",
language = "English",
volume = "41",
pages = "11731--11739",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "39",

}

RIS

TY - JOUR

T1 - Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore

AU - Urbaniak, Michael D.

AU - Muskett, Frederick W.

AU - Finucane, Michael D.

AU - Caddick, Stephen

AU - Woolfson, Derek N.

PY - 2002/10/1

Y1 - 2002/10/1

N2 - The natural complex Neocarzinostatin comprises a labile chromophore noncovalently bound to an 11.2 kDa protein. We present the first high-resolution structure of a novel complex derived from the recombinant apoprotein bound to a non-natural synthetic chromophore. Fluorescence and nuclear magnetic resonance spectroscopy were used to probe the strength and location of binding. Binding occurred in a location similar to that observed for the chromophore in the natural Neocarzinostatin complex, but with a distinct orientation. These results provide structural evidence that the apoprotein can readily accommodate small druglike entities, other than the natural chromophore within its binding cleft. The clinical use of the natural complex described by others, together with the results reported here, suggests potential applications for small molecule binding by apo-Neocarzinostatin.

AB - The natural complex Neocarzinostatin comprises a labile chromophore noncovalently bound to an 11.2 kDa protein. We present the first high-resolution structure of a novel complex derived from the recombinant apoprotein bound to a non-natural synthetic chromophore. Fluorescence and nuclear magnetic resonance spectroscopy were used to probe the strength and location of binding. Binding occurred in a location similar to that observed for the chromophore in the natural Neocarzinostatin complex, but with a distinct orientation. These results provide structural evidence that the apoprotein can readily accommodate small druglike entities, other than the natural chromophore within its binding cleft. The clinical use of the natural complex described by others, together with the results reported here, suggests potential applications for small molecule binding by apo-Neocarzinostatin.

KW - Antibiotics, Antineoplastic

KW - Apoproteins

KW - Binding Sites

KW - Circular Dichroism

KW - Crystallography, X-Ray

KW - Enediynes

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Recombinant Fusion Proteins

KW - Solutions

KW - Spectrometry, Fluorescence

KW - Zinostatin

U2 - 10.1021/bi0262146

DO - 10.1021/bi0262146

M3 - Journal article

C2 - 12269815

VL - 41

SP - 11731

EP - 11739

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 39

ER -