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| | <StructureSection load='4qpz' size='340' side='right'caption='[[4qpz]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4qpz' size='340' side='right'caption='[[4qpz]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qpz]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QPZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qpz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QPZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qq8|4qq8]]</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=4qpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpz OCA], [https://pdbe.org/4qpz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qpz RCSB], [https://www.ebi.ac.uk/pdbsum/4qpz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpz ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bznB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294 "Bacillus fluorescens liquefaciens" Flugge 1886])</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=4qpz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qpz OCA], [http://pdbe.org/4qpz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qpz RCSB], [http://www.ebi.ac.uk/pdbsum/4qpz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qpz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9F4L3_PSEFL Q9F4L3_PSEFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, D]] | + | [[Category: Pseudomonas fluorescens]] |
| - | [[Category: Shen, B W]] | + | [[Category: Baker D]] |
| - | [[Category: Siegel, J B]] | + | [[Category: Shen BW]] |
| - | [[Category: Stoddard, B L]] | + | [[Category: Siegel JB]] |
| - | [[Category: Formaldehyde lyase]] | + | [[Category: Stoddard BL]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q9F4L3_PSEFL
Publication Abstract from PubMed
We describe a computationally designed enzyme, formolase (FLS), which catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. The existence of FLS enables the design of a new carbon fixation pathway, the formolase pathway, consisting of a small number of thermodynamically favorable chemical transformations that convert formate into a three-carbon sugar in central metabolism. The formolase pathway is predicted to use carbon more efficiently and with less backward flux than any naturally occurring one-carbon assimilation pathway. When supplemented with enzymes carrying out the other steps in the pathway, FLS converts formate into dihydroxyacetone phosphate and other central metabolites in vitro. These results demonstrate how modern protein engineering and design tools can facilitate the construction of a completely new biosynthetic pathway.
Computational protein design enables a novel one-carbon assimilation pathway.,Siegel JB, Smith AL, Poust S, Wargacki AJ, Bar-Even A, Louw C, Shen BW, Eiben CB, Tran HM, Noor E, Gallaher JL, Bale J, Yoshikuni Y, Gelb MH, Keasling JD, Stoddard BL, Lidstrom ME, Baker D Proc Natl Acad Sci U S A. 2015 Mar 24;112(12):3704-9. doi:, 10.1073/pnas.1500545112. Epub 2015 Mar 9. PMID:25775555[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Siegel JB, Smith AL, Poust S, Wargacki AJ, Bar-Even A, Louw C, Shen BW, Eiben CB, Tran HM, Noor E, Gallaher JL, Bale J, Yoshikuni Y, Gelb MH, Keasling JD, Stoddard BL, Lidstrom ME, Baker D. Computational protein design enables a novel one-carbon assimilation pathway. Proc Natl Acad Sci U S A. 2015 Mar 24;112(12):3704-9. doi:, 10.1073/pnas.1500545112. Epub 2015 Mar 9. PMID:25775555 doi:http://dx.doi.org/10.1073/pnas.1500545112
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