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Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase.

Publication ,  Journal Article
Djordjevic, S; Roberts, DL; Wang, M; Shea, T; Camitta, MG; Masters, BS; Kim, JJ
Published in: Proc Natl Acad Sci U S A
April 11, 1995
Published version (DOI) Link to item

NADPH-cytochrome P450 reductase (CPR; NADPH:ferrihemoprotein reductase, EC 1.6.2.4) catalyzes the transfer of electrons to all known microsomal cytochromes P450. CPR is unique in that it is one of only two mammalian enzymes known to contain both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN), the other being the various isoforms of nitric oxide synthase. Similarities in amino acid sequence and in functional domain arrangement with other key flavoproteins, including nitric oxide synthase, make CPR an excellent prototype for studies of interactions between two flavin cofactors. We have obtained diffraction-quality crystals of rat liver CPR, expressed in Escherichia coli and solubilized by limited proteolysis with trypsin. The crystals were grown in Hepes buffer (pH 7.0), containing polyethylene glycol 4500 and NaCl. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions a = 103.3 A, b = 116.1 A, and c = 120.4 A. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vm is 2.54 A3/Da.

Duke Scholars

Michael G.W. Camitta
Author Michael G.W. Camitta Pediatrics, Cardiology

Published In

Proc Natl Acad Sci U S A

DOI

10.1073/pnas.92.8.3214

ISSN

0027-8424

Publication Date

April 11, 1995

Volume

92

Issue

8

Start / End Page

3214 / 3218

Location

United States

Related Subject Headings

  • Recombinant Proteins
  • Rats
  • NADPH-Ferrihemoprotein Reductase
  • Molecular Sequence Data
  • Liver
  • Escherichia coli
  • Crystallography, X-Ray
  • Crystallization
  • Animals
  • Amino Acid Sequence
 

Citation

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Djordjevic, S., Roberts, D. L., Wang, M., Shea, T., Camitta, M. G., Masters, B. S., & Kim, J. J. (1995). Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase. Proc Natl Acad Sci U S A, 92(8), 3214–3218. https://doi.org/10.1073/pnas.92.8.3214
Djordjevic, S., D. L. Roberts, M. Wang, T. Shea, M. G. Camitta, B. S. Masters, and J. J. Kim. “Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase.” Proc Natl Acad Sci U S A 92, no. 8 (April 11, 1995): 3214–18. https://doi.org/10.1073/pnas.92.8.3214.
Djordjevic S, Roberts DL, Wang M, Shea T, Camitta MG, Masters BS, et al. Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase. Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3214–8.
Djordjevic, S., et al. “Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase.” Proc Natl Acad Sci U S A, vol. 92, no. 8, Apr. 1995, pp. 3214–18. Pubmed, doi:10.1073/pnas.92.8.3214.
Djordjevic S, Roberts DL, Wang M, Shea T, Camitta MG, Masters BS, Kim JJ. Crystallization and preliminary x-ray studies of NADPH-cytochrome P450 reductase. Proc Natl Acad Sci U S A. 1995 Apr 11;92(8):3214–3218.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

10.1073/pnas.92.8.3214

ISSN

0027-8424

Publication Date

April 11, 1995

Volume

92

Issue

8

Start / End Page

3214 / 3218

Location

United States

Related Subject Headings

  • Recombinant Proteins
  • Rats
  • NADPH-Ferrihemoprotein Reductase
  • Molecular Sequence Data
  • Liver
  • Escherichia coli
  • Crystallography, X-Ray
  • Crystallization
  • Animals
  • Amino Acid Sequence