7ygk: Difference between revisions

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'''Unreleased structure'''


The entry 7ygk is ON HOLD  until Paper Publication
==Crystal structure of a secretory phospholipase A2 from Sciscionella marina==
<StructureSection load='7ygk' size='340' side='right'caption='[[7ygk]], [[Resolution|resolution]] 1.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ygk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sciscionella_marina Sciscionella marina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YGK FirstGlance]. <br>
</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=7ygk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ygk OCA], [https://pdbe.org/7ygk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ygk RCSB], [https://www.ebi.ac.uk/pdbsum/7ygk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ygk ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secretory phospholipase A(2) (sPLA(2)), which hydrolyzes the sn-2 acyl bond of lecithin in a Ca(2+)-dependent manner, is an important enzyme in the oil and oleochemical industries. However, most sPLA(2)s are not stable under process conditions. Therefore, a thermostable sPLA(2) was investigated in this study. A marine bacterial sPLA(2) isolated from Sciscionella marina (Sm-sPLA(2)) was catalytically active even after 5 h of incubation at high temperatures of up to 50 degrees C, which is outstanding compared with a representative bacterial sPLA(2) (i.e. sPLA(2) from Streptomyces violaceoruber; Sv-sPLA(2)). Consistent with this, the melting temperature of Sm-sPLA(2) was measured to be 7.7 degrees C higher than that of Sv-sPLA(2). Furthermore, Sm-sPLA(2) exhibited an improved biotransformation performance compared with Sv-sPLA(2) in the hydrolysis of soy lecithin to lysolecithin and free fatty acids at 50 degrees C. Structural and mutagenesis studies revealed that the Trp41-mediated anchoring of a Ca(2+)-binding loop into the rest of the protein body is directly linked to the thermal stability of Sm-sPLA(2). This finding provides a novel structural insight into the thermostability of sPLA(2) and could be applied to create mutant proteins with enhanced industrial potential.


Authors:  
Structural and functional characterization of a thermostable secretory phospholipase A(2) from Sciscionella marina and its application in liposome biotransformation.,Kang BG, Kwon SY, Lee HR, Hwang Y, Youn SY, Oh C, Park JB, Cha SS Acta Crystallogr D Struct Biol. 2023 Feb 1;79(Pt 2):188-197. doi: , 10.1107/S2059798323000384. Epub 2023 Feb 6. PMID:36762864<ref>PMID:36762864</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 7ygk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sciscionella marina]]
[[Category: Cha SS]]
[[Category: Kang BG]]
Retrieved from "https://proteopedia.org/7ygk"