Crystallization and Preliminary X-Ray Studies of NADPH-Cytochrome P450 Reductase

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 mononucle...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1995-04, Vol.92 (8), p.3214-3218
Hauptverfasser:	Djordjevic, S., Roberts, D. L., Wang, M., Shea, T., Camitta, M. G. W., Masters, B. S. S., Kim, J. J. P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Biochemistry Crystallization Crystallography, X-Ray Crystals Cytochromes Data collection Datasets Electrons Enzymes Escherichia coli - genetics Liver - enzymology Molecular Sequence Data NADPH-Ferrihemoprotein Reductase - chemistry NADPH-Ferrihemoprotein Reductase - genetics Oxides Proteins Rats Recombinant Proteins - chemistry
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container_title	Proceedings of the National Academy of Sciences - PNAS
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creator	Djordjevic, S. Roberts, D. L. Wang, M. Shea, T. Camitta, M. G. W. Masters, B. S. S. Kim, J. J. P.
description	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 P212121, with unit cell dimensions a= 103.3 Å, b=116.1 Å, and c=120.4 Å. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vmis 2.54 Å3/Da.
doi_str_mv	10.1073/pnas.92.8.3214
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The crystals were grown in Hepes buffer (pH 7.0), containing polyethylene glycol 4500 and NaCl. The crystals belong to the orthorhombic space group P212121, with unit cell dimensions a= 103.3 Å, b=116.1 Å, and c=120.4 Å. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vmis 2.54 Å3/Da.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.92.8.3214</identifier><identifier>PMID: 7724541</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Animals ; Biochemistry ; Crystallization ; Crystallography, X-Ray ; Crystals ; Cytochromes ; Data collection ; Datasets ; Electrons ; Enzymes ; Escherichia coli - genetics ; Liver - enzymology ; Molecular Sequence Data ; NADPH-Ferrihemoprotein Reductase - chemistry ; NADPH-Ferrihemoprotein Reductase - genetics ; Oxides ; Proteins ; Rats ; Recombinant Proteins - chemistry</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1995-04, Vol.92 (8), p.3214-3218</ispartof><rights>Copyright 1995 The National Academy of Sciences of the United States of America</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c457t-3c30aa754cacb799ac787e697c794599b2a0a6856233b3a8dadd8ae49e126133</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/92/8.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2367036$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2367036$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,729,782,786,805,887,27931,27932,53798,53800,58024,58257</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7724541$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Djordjevic, S.</creatorcontrib><creatorcontrib>Roberts, D. L.</creatorcontrib><creatorcontrib>Wang, M.</creatorcontrib><creatorcontrib>Shea, T.</creatorcontrib><creatorcontrib>Camitta, M. G. W.</creatorcontrib><creatorcontrib>Masters, B. S. S.</creatorcontrib><creatorcontrib>Kim, J. J. P.</creatorcontrib><title>Crystallization and Preliminary X-Ray Studies of NADPH-Cytochrome P450 Reductase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>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 P212121, with unit cell dimensions a= 103.3 Å, b=116.1 Å, and c=120.4 Å. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vmis 2.54 Å3/Da.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Cytochromes</subject><subject>Data collection</subject><subject>Datasets</subject><subject>Electrons</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Liver - enzymology</subject><subject>Molecular Sequence Data</subject><subject>NADPH-Ferrihemoprotein Reductase - chemistry</subject><subject>NADPH-Ferrihemoprotein Reductase - genetics</subject><subject>Oxides</subject><subject>Proteins</subject><subject>Rats</subject><subject>Recombinant Proteins - chemistry</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kb9P4zAYhi3ECQrHygRSJrbk_CtxLLGgcsBJ6K4CBjbrq-OCkRMX20FX_npStVRlYfLwPo_9-XsROia4IFiwX_MOYiFpUReMEr6DRgRLkldc4l00wpiKvOaU76ODGF8wxrKs8R7aE4LykpMRmozDIiZwzr5Dsr7LoGuySTDOtraDsMge8ztYZPepb6yJmZ9lfy8uJzf5eJG8fg6-NdmElzi7M02vE0TzE_2YgYvmaH0eooer3w_jm_z23_Wf8cVtrnkpUs40wwCi5Br0VEgJWtTCVFJoIXkp5ZQChqouK8rYlEHdQNPUYLg0hFaEsUN0vrp23k9b02jTpQBOzYNth6mVB6u-Jp19Vk_-TXFKWDXoZ2s9-NfexKRaG7VxDjrj-6iG_dCyImQAixWog48xmNnmCYLVsgC1LEBJqmq1LGAQTrcH2-DrjW_lS-8z3fbPvsvVrHcumf9pAE9W4EtMPmxIyiqBhx9-AHkiow8</recordid><startdate>19950411</startdate><enddate>19950411</enddate><creator>Djordjevic, S.</creator><creator>Roberts, D. 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L.</creatorcontrib><creatorcontrib>Wang, M.</creatorcontrib><creatorcontrib>Shea, T.</creatorcontrib><creatorcontrib>Camitta, M. G. W.</creatorcontrib><creatorcontrib>Masters, B. S. S.</creatorcontrib><creatorcontrib>Kim, J. J. P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Djordjevic, S.</au><au>Roberts, D. L.</au><au>Wang, M.</au><au>Shea, T.</au><au>Camitta, M. G. W.</au><au>Masters, B. S. S.</au><au>Kim, J. J. P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and Preliminary X-Ray Studies of NADPH-Cytochrome P450 Reductase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-04-11</date><risdate>1995</risdate><volume>92</volume><issue>8</issue><spage>3214</spage><epage>3218</epage><pages>3214-3218</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>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 P212121, with unit cell dimensions a= 103.3 Å, b=116.1 Å, and c=120.4 Å. If we assume that there are two molecules of the 72-kDa CPR polypeptide per asymmetric unit, the calculated value of Vmis 2.54 Å3/Da.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>7724541</pmid><doi>10.1073/pnas.92.8.3214</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record>
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subjects	Amino Acid Sequence Animals Biochemistry Crystallization Crystallography, X-Ray Crystals Cytochromes Data collection Datasets Electrons Enzymes Escherichia coli - genetics Liver - enzymology Molecular Sequence Data NADPH-Ferrihemoprotein Reductase - chemistry NADPH-Ferrihemoprotein Reductase - genetics Oxides Proteins Rats Recombinant Proteins - chemistry
title	Crystallization and Preliminary X-Ray Studies of NADPH-Cytochrome P450 Reductase
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