|
|
| (13 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1bi5.gif|left|200px]] | |
| | | | |
| - | <!-- | + | ==CHALCONE SYNTHASE FROM ALFALFA== |
| - | The line below this paragraph, containing "STRUCTURE_1bi5", creates the "Structure Box" on the page. | + | <StructureSection load='1bi5' size='340' side='right'caption='[[1bi5]], [[Resolution|resolution]] 1.56Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1bi5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BI5 FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> |
| - | {{STRUCTURE_1bi5| PDB=1bi5 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi5 OCA], [https://pdbe.org/1bi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bi5 RCSB], [https://www.ebi.ac.uk/pdbsum/1bi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bi5 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CHS2_MEDSA CHS2_MEDSA] The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.<ref>PMID:10653632</ref> <ref>PMID:11732902</ref> <ref>PMID:11959984</ref> <ref>PMID:15380179</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/1bi5_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bi5 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | 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. |
| | | | |
| - | '''CHALCONE SYNTHASE FROM ALFALFA'''
| + | 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<ref>PMID:10426957</ref> |
| - | | + | |
| - | | + | |
| - | ==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==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1BI5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Medicago_sativa Medicago sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BI5 OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1bi5" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10426957 10426957]
| + | *[[Chalcone synthase|Chalcone synthase]] |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Medicago sativa]] | | [[Category: Medicago sativa]] |
| - | [[Category: Naringenin-chalcone synthase]]
| + | [[Category: Bowman ME]] |
| - | [[Category: Single protein]]
| + | [[Category: Dixon RA]] |
| - | [[Category: Bowman, M E.]] | + | [[Category: Ferrer JL]] |
| - | [[Category: Dixon, R A.]] | + | [[Category: Jez JM]] |
| - | [[Category: Ferrer, J L.]] | + | [[Category: Noel JP]] |
| - | [[Category: Jez, J M.]] | + | |
| - | [[Category: Noel, J P.]] | + | |
| - | [[Category: Chalcone biosynthesis]]
| + | |
| - | [[Category: Polyketide synthase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:32:33 2008''
| + | |
| Structural highlights
Function
CHS2_MEDSA The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jez JM, Ferrer JL, Bowman ME, Dixon RA, Noel JP. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry. 2000 Feb 8;39(5):890-902. PMID:10653632
- ↑ Jez JM, Bowman ME, Noel JP. Structure-guided programming of polyketide chain-length determination in chalcone synthase. Biochemistry. 2001 Dec 11;40(49):14829-38. PMID:11732902
- ↑ Jez JM, Bowman ME, Noel JP. Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5319-24. PMID:11959984 doi:10.1073/pnas.082590499
- ↑ Austin MB, Bowman ME, Ferrer JL, Schroder J, Noel JP. An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketide synthases. Chem Biol. 2004 Sep;11(9):1179-94. PMID:15380179 doi:http://dx.doi.org/10.1016/j.chembiol.2004.05.024
- ↑ Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat Struct Biol. 1999 Aug;6(8):775-84. PMID:10426957 doi:http://dx.doi.org/10.1038/11553
|