Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase
Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 r...
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| Veröffentlicht in: | Protein science 1997-06, Vol.6 (6), p.1352-1357 |
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| container_title | Protein science |
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| creator | Kobe, Bostjan House, Colin M. Feil, Susanne C. Michell, Belinda J. Tiganis, Tony Parker, Michael W. Kemp, Bruce E. Cotton, Richard G.H. Jennings, Ian G. |
| description | Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme. |
| doi_str_mv | 10.1002/pro.5560060626 |
| format | Article |
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It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.5560060626</identifier><identifier>PMID: 9194198</identifier><language>eng</language><publisher>Bristol: Cold Spring Harbor Laboratory Press</publisher><subject>Animals ; Baculoviridae - genetics ; crystallization ; Crystallography, X-Ray ; Dimerization ; Enzyme Activation ; Humans ; Mass Spectrometry ; Peptide Fragments - chemistry ; Peptide Fragments - genetics ; Peptide Fragments - metabolism ; phenylalanine hydroxylase ; Phenylalanine Hydroxylase - chemistry ; Phenylalanine Hydroxylase - genetics ; Phenylalanine Hydroxylase - metabolism ; Phenylketonurias - etiology ; Phosphoproteins - chemistry ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; Phosphorylation ; Protein Conformation ; protein phosphorylation ; quaternary structure ; Rats ; Recombinant Proteins - chemistry ; Sequence Deletion ; Spodoptera - cytology ; X‐ray crystallography</subject><ispartof>Protein science, 1997-06, Vol.6 (6), p.1352-1357</ispartof><rights>Copyright © 2000 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4356-f6e11c7d25a6e6caa3264f1cfb69cd58b5e29505fa1064cc2d5ad76dd415040d3</citedby><cites>FETCH-LOGICAL-c4356-f6e11c7d25a6e6caa3264f1cfb69cd58b5e29505fa1064cc2d5ad76dd415040d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143721/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2143721/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27903,27904,45552,45553,46386,46810,53768,53770</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9194198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kobe, Bostjan</creatorcontrib><creatorcontrib>House, Colin M.</creatorcontrib><creatorcontrib>Feil, Susanne C.</creatorcontrib><creatorcontrib>Michell, Belinda J.</creatorcontrib><creatorcontrib>Tiganis, Tony</creatorcontrib><creatorcontrib>Parker, Michael W.</creatorcontrib><creatorcontrib>Kemp, Bruce E.</creatorcontrib><creatorcontrib>Cotton, Richard G.H.</creatorcontrib><creatorcontrib>Jennings, Ian G.</creatorcontrib><title>Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme.</description><subject>Animals</subject><subject>Baculoviridae - genetics</subject><subject>crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Enzyme Activation</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>phenylalanine hydroxylase</subject><subject>Phenylalanine Hydroxylase - chemistry</subject><subject>Phenylalanine Hydroxylase - genetics</subject><subject>Phenylalanine Hydroxylase - metabolism</subject><subject>Phenylketonurias - etiology</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Conformation</subject><subject>protein phosphorylation</subject><subject>quaternary structure</subject><subject>Rats</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sequence Deletion</subject><subject>Spodoptera - cytology</subject><subject>X‐ray crystallography</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEUhYMotT627oSu3E1NMkk62QgivkBQRMFdSJM7bWRmUpMZdfz1Rlt8bVyEcO_57rkJB6E9gscEY3q4CH7MucBYYEHFGhoSJmRWSPGwjoZYCpIVuSg20VaMjxhjRmg-QANJJCOyGKK3W5h1lW6db0a6sSMT-tjqqnJvy54vR4u5j-mEPmFgPykLf5qlD3X8gNvQNeazZV0NwZk0Dk2iKt24Bkbz3gb_muoIO2ij1FWE3dW9je7PTu9OLrKr6_PLk-OrzLCci6wUQIiZWMq1AGG0zqlgJTHlVEhjeTHlQCXHvNQEC2YMtVzbibCWEY4Ztvk2Olr6LrppDdZA0wZdqUVwtQ698tqp30rj5mrmnxUlLJ9QkgwOVgbBP3UQW1W7aKBKXwLfRTWRWMqUQALHS9AEH2OA8msJweojrVR79Z1WGtj_-bQvfBVP0uVSf3EV9P-4qZvb6x_e79bpp2k</recordid><startdate>199706</startdate><enddate>199706</enddate><creator>Kobe, Bostjan</creator><creator>House, Colin M.</creator><creator>Feil, Susanne C.</creator><creator>Michell, Belinda J.</creator><creator>Tiganis, Tony</creator><creator>Parker, Michael W.</creator><creator>Kemp, Bruce E.</creator><creator>Cotton, Richard G.H.</creator><creator>Jennings, Ian G.</creator><general>Cold Spring Harbor Laboratory Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199706</creationdate><title>Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase</title><author>Kobe, Bostjan ; House, Colin M. ; Feil, Susanne C. ; Michell, Belinda J. ; Tiganis, Tony ; Parker, Michael W. ; Kemp, Bruce E. ; Cotton, Richard G.H. ; Jennings, Ian G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4356-f6e11c7d25a6e6caa3264f1cfb69cd58b5e29505fa1064cc2d5ad76dd415040d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Baculoviridae - genetics</topic><topic>crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Enzyme Activation</topic><topic>Humans</topic><topic>Mass Spectrometry</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>phenylalanine hydroxylase</topic><topic>Phenylalanine Hydroxylase - chemistry</topic><topic>Phenylalanine Hydroxylase - genetics</topic><topic>Phenylalanine Hydroxylase - metabolism</topic><topic>Phenylketonurias - etiology</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - genetics</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Conformation</topic><topic>protein phosphorylation</topic><topic>quaternary structure</topic><topic>Rats</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sequence Deletion</topic><topic>Spodoptera - cytology</topic><topic>X‐ray crystallography</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kobe, Bostjan</creatorcontrib><creatorcontrib>House, Colin M.</creatorcontrib><creatorcontrib>Feil, Susanne C.</creatorcontrib><creatorcontrib>Michell, Belinda J.</creatorcontrib><creatorcontrib>Tiganis, Tony</creatorcontrib><creatorcontrib>Parker, Michael W.</creatorcontrib><creatorcontrib>Kemp, Bruce E.</creatorcontrib><creatorcontrib>Cotton, Richard G.H.</creatorcontrib><creatorcontrib>Jennings, Ian G.</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>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kobe, Bostjan</au><au>House, Colin M.</au><au>Feil, Susanne C.</au><au>Michell, Belinda J.</au><au>Tiganis, Tony</au><au>Parker, Michael W.</au><au>Kemp, Bruce E.</au><au>Cotton, Richard G.H.</au><au>Jennings, Ian G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>1997-06</date><risdate>1997</risdate><volume>6</volume><issue>6</issue><spage>1352</spage><epage>1357</epage><pages>1352-1357</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><abstract>Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C‐terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme.</abstract><cop>Bristol</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>9194198</pmid><doi>10.1002/pro.5560060626</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Baculoviridae - genetics crystallization Crystallography, X-Ray Dimerization Enzyme Activation Humans Mass Spectrometry Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism phenylalanine hydroxylase Phenylalanine Hydroxylase - chemistry Phenylalanine Hydroxylase - genetics Phenylalanine Hydroxylase - metabolism Phenylketonurias - etiology Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Phosphorylation Protein Conformation protein phosphorylation quaternary structure Rats Recombinant Proteins - chemistry Sequence Deletion Spodoptera - cytology X‐ray crystallography |
| title | Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase |
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