|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6h6v' size='340' side='right'caption='[[6h6v]], [[Resolution|resolution]] 2.66Å' scene=''> | | <StructureSection load='6h6v' size='340' side='right'caption='[[6h6v]], [[Resolution|resolution]] 2.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6h6v]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pelts Pelts]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H6V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H6V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6h6v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pelotomaculum_thermopropionicum_SI Pelotomaculum thermopropionicum SI]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H6V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.66Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UbiD, PTH_0496 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=370438 PELTS])</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=6h6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h6v OCA], [https://pdbe.org/6h6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h6v RCSB], [https://www.ebi.ac.uk/pdbsum/6h6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h6v ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6h6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h6v OCA], [http://pdbe.org/6h6v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h6v RCSB], [http://www.ebi.ac.uk/pdbsum/6h6v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h6v ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A5D4Z9_PELTS A5D4Z9_PELTS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pelts]] | + | [[Category: Pelotomaculum thermopropionicum SI]] |
| - | [[Category: Leys, D]] | + | [[Category: Leys D]] |
| - | [[Category: Payne, K A.P]] | + | [[Category: Payne KAP]] |
| - | [[Category: Decarboxylation]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Hmff]]
| + | |
| - | [[Category: Prfmn]]
| + | |
| - | [[Category: Thermophilic]]
| + | |
| - | [[Category: Ubid]]
| + | |
| Structural highlights
6h6v is a 6 chain structure with sequence from Pelotomaculum thermopropionicum SI. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.66Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
A5D4Z9_PELTS
Publication Abstract from PubMed
The biological production of FDCA is of considerable value as a potential replacement for petrochemical-derived monomers such as terephthalate, used in polyethylene terephthalate (PET) plastics. HmfF belongs to an uncharacterized branch of the prenylated flavin (prFMN) dependent UbiD family of reversible (de)carboxylases and is proposed to convert 2,5-furandicarboxylic acid (FDCA) to furoic acid in vivo. We present a detailed characterization of HmfF and demonstrate that HmfF can catalyze furoic acid carboxylation at elevated CO2 levels in vitro. We report the crystal structure of a thermophilic HmfF from Pelotomaculum thermopropionicum, revealing that the active site located above the prFMN cofactor contains a furoic acid/FDCA binding site composed of residues H296-R304-R331 specific to the HmfF branch of UbiD enzymes. Variants of the latter are compromised in activity, while H296N alters the substrate preference to pyrrole compounds. Solution studies and crystal structure determination of an engineered dimeric form of the enzyme revealed an unexpected key role for a UbiD family wide conserved Leu residue in activity. The structural insights into substrate and cofactor binding provide a template for further exploitation of HmfF in the production of FDCA plastic precursors and improve our understanding of catalysis by members of the UbiD enzyme family.
Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (FDCA).,Payne KAP, Marshall SA, Fisher K, Cliff MJ, Cannas DM, Yan C, Heyes DJ, Parker DA, Larrosa I, Leys D ACS Catal. 2019 Apr 5;9(4):2854-2865. doi: 10.1021/acscatal.8b04862. Epub 2019, Feb 15. PMID:31057985[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Payne KAP, Marshall SA, Fisher K, Cliff MJ, Cannas DM, Yan C, Heyes DJ, Parker DA, Larrosa I, Leys D. Enzymatic Carboxylation of 2-Furoic Acid Yields 2,5-Furandicarboxylic Acid (FDCA). ACS Catal. 2019 Apr 5;9(4):2854-2865. doi: 10.1021/acscatal.8b04862. Epub 2019, Feb 15. PMID:31057985 doi:http://dx.doi.org/10.1021/acscatal.8b04862
|
