1cml

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(New page: 200px<br /><applet load="1cml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cml, resolution 1.690&Aring;" /> '''CHALCONE SYNTHASE F...)
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caption="1cml, resolution 1.690&Aring;" />
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'''CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA'''<br />
'''CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA'''<br />
==Overview==
==Overview==
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Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid, antimicrobial phytoalexins and anthocyanin pigments in plants. It produces, chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A, thioesters into a polyketide reaction intermediate that cyclizes. The, crystal structures of CHS alone and complexed with substrate and product, analogs reveal the active site architecture that defines the sequence and, chemistry of multiple decarboxylation and condensation reactions and, provides a molecular understanding of the cyclization reaction leading to, chalcone synthesis. The structure of CHS complexed with resveratrol also, suggests how stilbene synthase, a related enzyme, uses the same substrates, and an alternate cyclization pathway to form resveratrol. By using the, three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product, specificity. The structure elucidates the chemical basis of plant, polyketide biosynthesis and provides a framework for engineering CHS-like, enzymes to produce new products.
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Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid antimicrobial phytoalexins and anthocyanin pigments in plants. It produces chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A thioesters into a polyketide reaction intermediate that cyclizes. The crystal structures of CHS alone and complexed with substrate and product analogs reveal the active site architecture that defines the sequence and chemistry of multiple decarboxylation and condensation reactions and provides a molecular understanding of the cyclization reaction leading to chalcone synthesis. The structure of CHS complexed with resveratrol also suggests how stilbene synthase, a related enzyme, uses the same substrates and an alternate cyclization pathway to form resveratrol. By using the three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product specificity. The structure elucidates the chemical basis of plant polyketide biosynthesis and provides a framework for engineering CHS-like enzymes to produce new products.
==About this Structure==
==About this Structure==
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1CML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa] with SO4, MLC and PIN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CML OCA].
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1CML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MLC:'>MLC</scene> and <scene name='pdbligand=PIN:'>PIN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CML OCA].
==Reference==
==Reference==
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[[Category: Naringenin-chalcone synthase]]
[[Category: Naringenin-chalcone synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowman, M.E.]]
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[[Category: Bowman, M E.]]
[[Category: Dixon, R.]]
[[Category: Dixon, R.]]
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[[Category: Ferrer, J.L.]]
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[[Category: Ferrer, J L.]]
[[Category: Jez, J.]]
[[Category: Jez, J.]]
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[[Category: Noel, J.P.]]
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[[Category: Noel, J P.]]
[[Category: MLC]]
[[Category: MLC]]
[[Category: PIN]]
[[Category: PIN]]
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[[Category: polyketide synthase]]
[[Category: polyketide synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:35:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:34 2008''

Revision as of 10:07, 21 February 2008


1cml, resolution 1.690Å

Drag the structure with the mouse to rotate

CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH MALONYL-COA

Overview

Chalcone synthase (CHS) is pivotal for the biosynthesis of flavonoid antimicrobial phytoalexins and anthocyanin pigments in plants. It produces chalcone by condensing one p-coumaroyl- and three malonyl-coenzyme A thioesters into a polyketide reaction intermediate that cyclizes. The crystal structures of CHS alone and complexed with substrate and product analogs reveal the active site architecture that defines the sequence and chemistry of multiple decarboxylation and condensation reactions and provides a molecular understanding of the cyclization reaction leading to chalcone synthesis. The structure of CHS complexed with resveratrol also suggests how stilbene synthase, a related enzyme, uses the same substrates and an alternate cyclization pathway to form resveratrol. By using the three-dimensional structure and the large database of CHS-like sequences, we can identify proteins likely to possess novel substrate and product specificity. The structure elucidates the chemical basis of plant polyketide biosynthesis and provides a framework for engineering CHS-like enzymes to produce new products.

About this Structure

1CML is a Single protein structure of sequence from Medicago sativa with , and as ligands. Active as Naringenin-chalcone synthase, with EC number 2.3.1.74 Full crystallographic information is available from OCA.

Reference

Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis., Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP, Nat Struct Biol. 1999 Aug;6(8):775-84. PMID:10426957

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