Crystallization and phasing of alanine dehydrogenase from Archaeoglobus fulgidus
Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolutionary links to the broad ornithine cyclodeaminas...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-12, Vol.59 (12), p.2328-2331 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Smith, Natasha Mayhew, Martin Robinson, Howard Héroux, Annie Charlton, David Holden, Marcia J. Gallagher, D. T. |
| description | Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolutionary links to the broad ornithine cyclodeaminase/μ‐crystallin family, which includes human thyroid hormone binding protein, which has 30% sequence identity to the A. fulgidus gene. The enzyme has been cloned, shown to catalyze the NAD‐dependent interconversion of alanine and pyruvate and crystallized in several forms. Although the purified protein crystallized readily under many conditions, most of the crystals diffracted weakly or not at all. One polymorph growing in space group P212121 has non‐crystallographic symmetry that becomes crystallographic, changing the space group to P21212, upon binding iridium or samarium. Before and after derivatization, these crystals diffracted to 2.5 Å using synchrotron radiation. Multiwavelength diffraction data were collected from the non‐isomorphous iridium derivative, enabling structure determination. |
| doi_str_mv | 10.1107/S0907444903021565 |
| format | Article |
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T.</creator><creatorcontrib>Smith, Natasha ; Mayhew, Martin ; Robinson, Howard ; Héroux, Annie ; Charlton, David ; Holden, Marcia J. ; Gallagher, D. T.</creatorcontrib><description>Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolutionary links to the broad ornithine cyclodeaminase/μ‐crystallin family, which includes human thyroid hormone binding protein, which has 30% sequence identity to the A. fulgidus gene. The enzyme has been cloned, shown to catalyze the NAD‐dependent interconversion of alanine and pyruvate and crystallized in several forms. Although the purified protein crystallized readily under many conditions, most of the crystals diffracted weakly or not at all. One polymorph growing in space group P212121 has non‐crystallographic symmetry that becomes crystallographic, changing the space group to P21212, upon binding iridium or samarium. Before and after derivatization, these crystals diffracted to 2.5 Å using synchrotron radiation. Multiwavelength diffraction data were collected from the non‐isomorphous iridium derivative, enabling structure determination.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444903021565</identifier><identifier>PMID: 14646110</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Alanine Dehydrogenase ; Amino Acid Oxidoreductases - chemistry ; Amino Acid Oxidoreductases - genetics ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeoglobus fulgidus - enzymology ; Archaeoglobus fulgidus - genetics ; crystal growth ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Iridium - chemistry ; multiwavelength anomalous dispersion ; NAD ; ornithine cyclodeaminase ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Samarium - chemistry ; Synchrotrons</subject><ispartof>Acta crystallographica. 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T.</creatorcontrib><title>Crystallization and phasing of alanine dehydrogenase from Archaeoglobus fulgidus</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolutionary links to the broad ornithine cyclodeaminase/μ‐crystallin family, which includes human thyroid hormone binding protein, which has 30% sequence identity to the A. fulgidus gene. The enzyme has been cloned, shown to catalyze the NAD‐dependent interconversion of alanine and pyruvate and crystallized in several forms. Although the purified protein crystallized readily under many conditions, most of the crystals diffracted weakly or not at all. One polymorph growing in space group P212121 has non‐crystallographic symmetry that becomes crystallographic, changing the space group to P21212, upon binding iridium or samarium. Before and after derivatization, these crystals diffracted to 2.5 Å using synchrotron radiation. Multiwavelength diffraction data were collected from the non‐isomorphous iridium derivative, enabling structure determination.</description><subject>Alanine Dehydrogenase</subject><subject>Amino Acid Oxidoreductases - chemistry</subject><subject>Amino Acid Oxidoreductases - genetics</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeoglobus fulgidus - enzymology</subject><subject>Archaeoglobus fulgidus - genetics</subject><subject>crystal growth</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Dimerization</subject><subject>Iridium - chemistry</subject><subject>multiwavelength anomalous dispersion</subject><subject>NAD</subject><subject>ornithine cyclodeaminase</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Samarium - chemistry</subject><subject>Synchrotrons</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0E4v0BbFBW7AKe2LGdZVWgICHeCMHGcpJJa0jjYjeC8vWkagVILFjNLO45urqE7AE9BKDy6I5mVHLOM8poAqlIV8gmsCyLKeVy9de_QbZCeKGUJgmT62QDuOCiU2yS676fhampa_tpptY1kWnKaDIywTbDyFWRqU1jG4xKHM1K74bYmIBR5d046vliZNANa5e3IaraemjLNuyQtcrUAXeXd5s8nJ7c98_ii6vBeb93ERdMcRHnWQ6FwhKUoVWuBE9AcRRAMwkcpEAQlawUMkhUyjE1nBcyKTIjISlSlrNtcrDwTrx7azFM9diGAuuuL7o26LmGCyq6ICyChXcheKz0xNux8TMNVM9n1H9m7Jj9pbzNx1j-EMvduoBaBN5tjbP_jbr3dHz9QCGZ94kXqA1T_PhGjX_VQjKZ6sfLgb65fYZL1T_WnH0BcE6MEQ</recordid><startdate>200312</startdate><enddate>200312</enddate><creator>Smith, Natasha</creator><creator>Mayhew, Martin</creator><creator>Robinson, Howard</creator><creator>Héroux, Annie</creator><creator>Charlton, David</creator><creator>Holden, Marcia J.</creator><creator>Gallagher, D. T.</creator><general>Munksgaard International Publishers</general><scope>BSCLL</scope><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></search><sort><creationdate>200312</creationdate><title>Crystallization and phasing of alanine dehydrogenase from Archaeoglobus fulgidus</title><author>Smith, Natasha ; Mayhew, Martin ; Robinson, Howard ; Héroux, Annie ; Charlton, David ; Holden, Marcia J. ; Gallagher, D. T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3846-b9b1c8ed18a0fb8642184e6109714176e16f7f8e312854e5a44c72c9a712c53b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Alanine Dehydrogenase</topic><topic>Amino Acid Oxidoreductases - chemistry</topic><topic>Amino Acid Oxidoreductases - genetics</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeoglobus fulgidus - enzymology</topic><topic>Archaeoglobus fulgidus - genetics</topic><topic>crystal growth</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Dimerization</topic><topic>Iridium - chemistry</topic><topic>multiwavelength anomalous dispersion</topic><topic>NAD</topic><topic>ornithine cyclodeaminase</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Samarium - chemistry</topic><topic>Synchrotrons</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smith, Natasha</creatorcontrib><creatorcontrib>Mayhew, Martin</creatorcontrib><creatorcontrib>Robinson, Howard</creatorcontrib><creatorcontrib>Héroux, Annie</creatorcontrib><creatorcontrib>Charlton, David</creatorcontrib><creatorcontrib>Holden, Marcia J.</creatorcontrib><creatorcontrib>Gallagher, D. 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D</addtitle><date>2003-12</date><risdate>2003</risdate><volume>59</volume><issue>12</issue><spage>2328</spage><epage>2331</epage><pages>2328-2331</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Alanine dehydrogenase (AlaDH) from the hyperthermophilic archaeon Archaeoglobus fulgidus is a dimer of 35 kDa chains. The archaeal enzyme appears to represent a new class of AlaDH that is not homologous to bacterial AlaDH enzymes, but has close evolutionary links to the broad ornithine cyclodeaminase/μ‐crystallin family, which includes human thyroid hormone binding protein, which has 30% sequence identity to the A. fulgidus gene. The enzyme has been cloned, shown to catalyze the NAD‐dependent interconversion of alanine and pyruvate and crystallized in several forms. Although the purified protein crystallized readily under many conditions, most of the crystals diffracted weakly or not at all. One polymorph growing in space group P212121 has non‐crystallographic symmetry that becomes crystallographic, changing the space group to P21212, upon binding iridium or samarium. Before and after derivatization, these crystals diffracted to 2.5 Å using synchrotron radiation. Multiwavelength diffraction data were collected from the non‐isomorphous iridium derivative, enabling structure determination.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>14646110</pmid><doi>10.1107/S0907444903021565</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; Access via Wiley Online Library; Alma/SFX Local Collection |
| subjects | Alanine Dehydrogenase Amino Acid Oxidoreductases - chemistry Amino Acid Oxidoreductases - genetics Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeoglobus fulgidus - enzymology Archaeoglobus fulgidus - genetics crystal growth Crystallization Crystallography, X-Ray Dimerization Iridium - chemistry multiwavelength anomalous dispersion NAD ornithine cyclodeaminase Recombinant Proteins - chemistry Recombinant Proteins - genetics Samarium - chemistry Synchrotrons |
| title | Crystallization and phasing of alanine dehydrogenase from Archaeoglobus fulgidus |
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