View source for 9lvn


==Crystal structure of phospholipase D SkPLD (Streptomyces klenkii)==
<StructureSection load='9lvn' size='340' side='right'caption='[[9lvn]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9lvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces Streptomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9LVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9LVN 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]] 1.88&#8491;</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=9lvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9lvn OCA], [https://pdbe.org/9lvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9lvn RCSB], [https://www.ebi.ac.uk/pdbsum/9lvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9lvn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3B0B5W1_9ACTN A0A3B0B5W1_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
This study aimed to decipher the structure-function relationship of Streptomyces klenkii phospholipase D (SkPLD) and leverage its transphosphatidylation activity for synthesizing functional phospholipids in milk fat systems. Crystallography and mutagenesis analyses identified dynamic loops (c-f) as key mediators of substrate recognition. Targeted constraints, including proline substitution in loop (c) and disulfide bonds in loops (d/e), impaired transphosphatidylation, with loop (f) being essential for catalysis. Moreover, SkPLD employs dual HKD motifs: His167 initiates nucleophilic attack, while His440 activates acceptors, stabilized by Tyr459, Asp199, and Asp465. Hydrophobic residues and Ala122/Asn457 determine phospholipid alkyl side chain orientation. We achieved direct phosphatidylserine (8.1 mg/mL), phosphatidylethanolamine (42.8 mg/mL), and phosphatidylglycerol (13.2 mg/mL) synthesis in milk fat globule membranes using SkPLD, from initial levels of 1.5, 26.7, and 0 mg/mL, bypassing solvent-based systems. This work provides a mechanistic framework for Streptomyces phospholipase D catalysis and establishes an enzymatic strategy for functional phospholipid enrichment in dairy products.

Dynamic loops and active site mediate substrate recognition of Streptomyces phospholipase D and its functional phospholipid synthesis in dairy system.,Wu L, Feng C, Li T, Cao J, Zhao H, Liang S, Rui M, Pan L, Hu R Food Res Int. 2026 Jan;223(Pt 1):117865. doi: 10.1016/j.foodres.2025.117865. Epub , 2025 Nov 12. PMID:41352798<ref>PMID:41352798</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9lvn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces]]
[[Category: Feng CH]]
[[Category: Hu RK]]