6vby
From Proteopedia
(Difference between revisions)
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==Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor== | ==Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor== | ||
| - | <StructureSection load='6vby' size='340' side='right'caption='[[6vby]]' scene=''> | + | <StructureSection load='6vby' size='340' side='right'caption='[[6vby]], [[Resolution|resolution]] 1.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VBY OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6vby]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sorghum_bicolor Sorghum bicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VBY FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=6vby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vby OCA], [https://pdbe.org/6vby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vby RCSB], [https://www.ebi.ac.uk/pdbsum/6vby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vby ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TCMO_SORBI TCMO_SORBI] Catalyzes the first oxidative step of the phenylpropanoid pathway in higher plants by transforming trans-cinnamate into p-coumarate (PubMed:32332088). The compounds formed by this pathway are essential components for lignification, pollination, and defense against ultraviolet light, predators and pathogens (PubMed:32332088). Can also use 2-naphthoic acid as substrate (PubMed:32332088).<ref>PMID:32332088</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cinnamate 4-hydroxylase (C4H; CYP73A) is a cytochrome P450 monooxygenase associated externally with the endoplasmic reticulum of plant cells. The enzyme uses NADPH-cytochrome P450 reductase as a donor of electrons and hydroxylates cinnamic acid to form 4-coumaric acid in phenylpropanoid metabolism. In order to better understand the structure and function of this unique class of plant P450 enzymes, we have characterized the enzyme C4H1 from lignifying tissues of sorghum (Sorghum bicolor), encoded by Sobic.002G126600 Here we report the 1.7 A resolution crystal structure of CYP73A33. The obtained structural information, along with the results of the steady-state kinetic analysis and the absorption spectroscopy titration, displays a high degree of similarity of the structural and functional features of C4H to those of other P450 proteins. Our data also suggest the presence of a putative allosteric substrate-binding site in a hydrophobic pocket on the enzyme surface. In addition, comparing the newly resolved structure with those of well-investigated cytochromes P450 from mammals and bacteria enabled us to identify those residues of critical functional importance and revealed a unique sequence signature that is potentially responsible for substrate specificity and catalytic selectivity of C4H. | ||
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| + | Structure and Function of the Cytochrome P450 Monooxygenase Cinnamate 4-hydroxylase from Sorghum bicolor.,Zhang B, Lewis KM, Abril A, Davydov DR, Vermerris W, Sattler SE, Kang C Plant Physiol. 2020 Jul;183(3):957-973. doi: 10.1104/pp.20.00406. Epub 2020 Apr, 24. PMID:32332088<ref>PMID:32332088</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6vby" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Sorghum bicolor]] | ||
[[Category: Kang C]] | [[Category: Kang C]] | ||
[[Category: Lewis KM]] | [[Category: Lewis KM]] | ||
[[Category: Zhang B]] | [[Category: Zhang B]] | ||
Current revision
Cinnamate 4-hydroxylase (C4H1) from Sorghum bicolor
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