9lj9: Difference between revisions
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==Crystal structure of a bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase== | |||
<StructureSection load='9lj9' size='340' side='right'caption='[[9lj9]], [[Resolution|resolution]] 2.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9lj9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LJ9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.64Å</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=SO4:SULFATE+ION'>SO4</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=9lj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lj9 OCA], [https://pdbe.org/9lj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lj9 RCSB], [https://www.ebi.ac.uk/pdbsum/9lj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lj9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O59601_PYRHO O59601_PYRHO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
3-Hexulose-6-phosphate synthase, a key enzyme in the ribulose monophosphate pathway, plays a central role in formaldehyde assimilation and detoxification, offering great potential for third-generation green biomanufacturing. In this study, we determined the crystal structure of HPS from Pyrococcus horikoshii at a 2.64 A resolution. Combined approaches, including molecular docking, multiple sequence alignment, and alanine scanning, identified critical catalytic residues. Two variants, T136C and V186W, exhibited over 6-fold higher activity than the wild type. Molecular dynamics simulations indicated increased structural rigidity and enhanced stability upon substrate (d-ribulose-5-phosphate) binding, along with significantly improved binding energies. Furthermore, an enzyme cascade converting d-xylose and formaldehyde to d-fructose-6-phosphate was constructed to evaluate the HPS activity under optimized conditions. These findings provide insights into the catalytic mechanism of HPS and offer a basis for its application in one-carbon bioconversion. | |||
Crystal Structure, Mutations, and Catalytic Properties of 3-Hexulose-6-phosphate Synthase from Pyrococcus horikoshii.,Li Y, Liu Y, Ji Y, Xu H, Wang H, Feng Y, Liu L J Agric Food Chem. 2025 Jul 9;73(27):17103-17113. doi: 10.1021/acs.jafc.5c02365. , Epub 2025 Jun 28. PMID:40580126<ref>PMID:40580126</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9lj9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii OT3]] | |||
[[Category: Feng Y]] | |||
[[Category: Ji Y]] | |||
[[Category: Li YX]] | |||
[[Category: Liu L]] | |||
[[Category: Wang H]] | |||
Latest revision as of 05:56, 1 October 2025
Crystal structure of a bifunctional 3-hexulose-6-phosphate synthase/6-phospho-3-hexuloisomerase
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