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1chw

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CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH HEXANOYL-COA

Structural highlights

1chw is a 2 chain structure with sequence from Medicago sativa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1chw"

@@ Line 3: / Line 3: @@
 <StructureSection load='1chw' size='340' side='right'caption='[[1chw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1chw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alfalfa Alfalfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1chw]] is a 2 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=1CHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CHW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HXC:HEXANOYL-COENZYME+A'>HXC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Naringenin-chalcone_synthase Naringenin-chalcone synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.74 2.3.1.74] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HXC:HEXANOYL-COENZYME+A'>HXC</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1chw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1chw OCA], [https://pdbe.org/1chw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1chw RCSB], [https://www.ebi.ac.uk/pdbsum/1chw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1chw 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>
+[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]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Alfalfa]]
 [[Category: Large Structures]]
-[[Category: Naringenin-chalcone synthase]]
+[[Category: Medicago sativa]]
-[[Category: Bowman, M E]]
+[[Category: Bowman ME]]
-[[Category: Dixon, R]]
+[[Category: Dixon R]]
-[[Category: Ferrer, J L]]
+[[Category: Ferrer J-L]]
-[[Category: Jez, J]]
+[[Category: Jez J]]
-[[Category: Noel, J P]]
+[[Category: Noel JP]]
-[[Category: Chalcone biosynthesis]]
-[[Category: Polyketide synthase]]
-[[Category: Transferase]]

1chw

From Proteopedia

Current revision

CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH HEXANOYL-COA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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