View source for 26vk


==Crystal structure of Dihydroxyacetone kinase from Komagataella pastoris==
<StructureSection load='26vk' size='340' side='right'caption='[[26vk]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[26vk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_pastoris Komagataella pastoris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=26VK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=26VK 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]] 2.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=26vk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=26vk OCA], [https://pdbe.org/26vk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=26vk RCSB], [https://www.ebi.ac.uk/pdbsum/26vk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=26vk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DAK_PICPA DAK_PICPA] Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dihydroxyacetone kinase (DAK) catalyzes the ATP-dependent phosphorylation of dihydroxyacetone (DHA) and is an important enzyme in artificial starch synthesis. Here, we report the crystal structure of a methylotrophic yeast DAK from Komagataella phaffii (formly Pichia pastoris, PpDAK). ATP was observed at a non-canonical site distinct from the canonical bacterial ATP-binding pocket. Docking further suggested that the canonical pocket remains accessible, indicating flexibility in ATP recognition. Sequence and phylogenetic analyses show that PpDAK clusters within a distinct methylotrophic yeast lineage and that residues surrounding the non-canonical ATP-binding site are conserved among methylotrophic yeasts. In addition, Mg(2+) ions were identified in some substrate-binding pockets and docking suggested substantial overlap between Mg(2+) and the predicted DHA-binding position. Together, these findings provide structural insights into ATP recognition in fungal DAKs and a framework for future functional studies and enzyme engineering.

Crystal structure of a fungal dihydroxyacetone kinase reveals a non-canonical ATP-binding site.,Wei H, Chen Y, Zhang F, Li Q, Liu P, Cai T, Liu W Biochem Biophys Res Commun. 2026 Jul 13;830:154274. doi: , 10.1016/j.bbrc.2026.154274. PMID:42442090<ref>PMID:42442090</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 26vk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Komagataella pastoris]]
[[Category: Large Structures]]
[[Category: Cai T]]
[[Category: Chen YY]]
[[Category: Li Q]]
[[Category: Liu WD]]
[[Category: Wei HL]]