Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase1[W][OA]
Identifieur interne : 000C91 ( Pmc/Corpus ); précédent : 000C90; suivant : 000C92Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase1[W][OA]
Auteurs : Fu-Lien Hsieh ; Tao-Hsin Chang ; Tzu-Ping Ko ; Andrew H.-J. WangSource :
- Plant Physiology [ 0032-0889 ] ; 2011.
Abstract
Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (
Url:
DOI: 10.1104/pp.110.168799
PubMed: 21220764
PubMed Central: 3046570
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase<xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn4"><sup>[W]</sup></xref><xref ref-type="author-notes" rid="fn5"><sup>[OA]</sup></xref></title><author><name sortKey="Hsieh, Fu Lien" sort="Hsieh, Fu Lien" uniqKey="Hsieh F" first="Fu-Lien" last="Hsieh">Fu-Lien Hsieh</name></author><author><name sortKey="Chang, Tao Hsin" sort="Chang, Tao Hsin" uniqKey="Chang T" first="Tao-Hsin" last="Chang">Tao-Hsin Chang</name></author><author><name sortKey="Ko, Tzu Ping" sort="Ko, Tzu Ping" uniqKey="Ko T" first="Tzu-Ping" last="Ko">Tzu-Ping Ko</name></author><author><name sortKey="Wang, Andrew H J" sort="Wang, Andrew H J" uniqKey="Wang A" first="Andrew H.-J." last="Wang">Andrew H.-J. Wang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21220764</idno><idno type="pmc">3046570</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3046570</idno><idno type="RBID">PMC:3046570</idno><idno type="doi">10.1104/pp.110.168799</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000C91</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase<xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn4"><sup>[W]</sup></xref><xref ref-type="author-notes" rid="fn5"><sup>[OA]</sup></xref></title><author><name sortKey="Hsieh, Fu Lien" sort="Hsieh, Fu Lien" uniqKey="Hsieh F" first="Fu-Lien" last="Hsieh">Fu-Lien Hsieh</name></author><author><name sortKey="Chang, Tao Hsin" sort="Chang, Tao Hsin" uniqKey="Chang T" first="Tao-Hsin" last="Chang">Tao-Hsin Chang</name></author><author><name sortKey="Ko, Tzu Ping" sort="Ko, Tzu Ping" uniqKey="Ko T" first="Tzu-Ping" last="Ko">Tzu-Ping Ko</name></author><author><name sortKey="Wang, Andrew H J" sort="Wang, Andrew H J" uniqKey="Wang A" first="Andrew H.-J." last="Wang">Andrew H.-J. Wang</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (<italic>Arabidopsis thaliana</italic>) is identified as a trans-type polyprenyl pyrophosphate synthase (AtPPPS), which forms a trans-double bond during each homoallylic substrate condensation, rather than a homomeric C<sub>10</sub>-geranyl pyrophosphate synthase as originally proposed. Biochemical and genetic complementation analyses indicate that AtPPPS synthesizes C<sub>25</sub> to C<sub>45</sub> medium/long-chain products. Its close relationship to other long-chain PTSs is also uncovered by phylogenetic analysis. A mutant of contiguous surface polar residues was produced by replacing four charged surface amino acids with alanines to facilitate the crystallization of the enzyme. The crystal structures of AtPPPS determined here in apo and ligand-bound forms further reveal an active-site cavity sufficient to accommodate the medium/long-chain products. The two monomers in each dimer adopt different conformations at the entrance of the active site depending on the binding of substrates. Taken together, these results suggest that AtPPPS is endowed with a unique functionality among the known PTSs.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-id journal-id-type="hwp">plantphysiol</journal-id><journal-id journal-id-type="publisher-id">aspb</journal-id><journal-title-group><journal-title>Plant Physiology</journal-title></journal-title-group><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn><publisher><publisher-name>American Society of Plant Biologists</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21220764</article-id><article-id pub-id-type="pmc">3046570</article-id><article-id pub-id-type="publisher-id">168799</article-id><article-id pub-id-type="doi">10.1104/pp.110.168799</article-id><article-categories><subj-group><subject>Article</subject></subj-group><subj-group subj-group-type="heading"><subject>Biochemical Processes and Macromolecular Structures</subject></subj-group></article-categories><title-group><article-title>Structure and Mechanism of an Arabidopsis Medium/Long-Chain-Length Prenyl Pyrophosphate Synthase<xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn4"><sup>[W]</sup></xref><xref ref-type="author-notes" rid="fn5"><sup>[OA]</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Hsieh</surname><given-names>Fu-Lien</given-names></name><xref ref-type="author-notes" rid="fn2"><sup>2</sup></xref><xref ref-type="author-notes" rid="fn3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Chang</surname><given-names>Tao-Hsin</given-names></name><xref ref-type="author-notes" rid="fn2"><sup>2</sup></xref><xref ref-type="author-notes" rid="fn3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ko</surname><given-names>Tzu-Ping</given-names></name></contrib><contrib contrib-type="author"><name><surname>Wang</surname><given-names>Andrew H.-J.</given-names></name><xref ref-type="corresp" rid="cor1"><sup>*</sup></xref></contrib></contrib-group><aff>Institute of Biological Chemistry (F.-L.H., T.-H.C., T.-P.K., A.H.-J.W.) and Core Facilities for Protein Production and X-Ray Structural Analysis (T.-P.K., A.H.-J.W.), Academia Sinica, Taipei 115, Taiwan; Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan (F.-L.H., A.H.-J.W.)</aff><author-notes><corresp id="cor1"><label>*</label>Corresponding author; e-mail <email>ahjwang@gate.sinica.edu.tw</email>.</corresp><fn id="fn1"><label>1</label><p>This work was supported by Academia Sinica and the Core Facility for Protein Production and X-Ray Structural Analysis (grant no. NSC97–3112–B–001–035–B4 to A.H.-J.W.). The Protein Crystallography Facility of the National Synchrotron Radiation Research Center is supported by the National Research Program for Genomic Medicine.</p></fn><fn id="fn2" fn-type="equal"><label>2</label><p>These authors contributed equally to the article.</p></fn><fn id="fn3"><label>3</label><p>Present address: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.</p></fn><fn><p>The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (<ext-link ext-link-type="uri" xlink:href="www.plantphysiol.org">www.plantphysiol.org</ext-link>) is: Andrew H.-J. Wang (<email>ahjwang@gate.sinica.edu.tw</email>).</p></fn><fn id="fn4"><label>[W]</label><p>The online version of this article contains Web-only data.</p></fn><fn id="fn5"><label>[OA]</label><p>Open Access articles can be viewed online without a subscription.</p></fn><fn><p><ext-link ext-link-type="uri" xlink:href="www.plantphysiol.org/cgi/doi/10.1104/pp.110.168799">www.plantphysiol.org/cgi/doi/10.1104/pp.110.168799</ext-link></p></fn></author-notes><pmc-comment>Fake ppub date generated by PMC from publisher pub-date/@pub-type='epub-ppub' </pmc-comment>
<pub-date pub-type="ppub"><month>3</month><year>2011</year></pub-date><pub-date pub-type="epub"><day>10</day><month>1</month><year>2011</year></pub-date><pub-date pub-type="pmc-release"><day>10</day><month>1</month><year>2011</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
<volume>155</volume><issue>3</issue><fpage>1079</fpage><lpage>1090</lpage><history><date date-type="received"><day>2</day><month>11</month><year>2010</year></date><date date-type="accepted"><day>6</day><month>1</month><year>2011</year></date></history><permissions><copyright-statement>© 2011 American Society of Plant Biologists</copyright-statement><copyright-year>2011</copyright-year></permissions><abstract><p>Prenyltransferases (PTSs) are involved in the biosynthesis of terpenes with diverse functions. Here, a novel PTS from Arabidopsis (<italic>Arabidopsis thaliana</italic>) is identified as a trans-type polyprenyl pyrophosphate synthase (AtPPPS), which forms a trans-double bond during each homoallylic substrate condensation, rather than a homomeric C<sub>10</sub>-geranyl pyrophosphate synthase as originally proposed. Biochemical and genetic complementation analyses indicate that AtPPPS synthesizes C<sub>25</sub> to C<sub>45</sub> medium/long-chain products. Its close relationship to other long-chain PTSs is also uncovered by phylogenetic analysis. A mutant of contiguous surface polar residues was produced by replacing four charged surface amino acids with alanines to facilitate the crystallization of the enzyme. The crystal structures of AtPPPS determined here in apo and ligand-bound forms further reveal an active-site cavity sufficient to accommodate the medium/long-chain products. The two monomers in each dimer adopt different conformations at the entrance of the active site depending on the binding of substrates. Taken together, these results suggest that AtPPPS is endowed with a unique functionality among the known PTSs.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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