View source for 9wyx


==Cryo-EM structure of PbSS==
<StructureSection load='9wyx' size='340' side='right'caption='[[9wyx]], [[Resolution|resolution]] 3.04&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9wyx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_brasilianum Penicillium brasilianum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9WYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9WYX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.04&#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=9wyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9wyx OCA], [https://pdbe.org/9wyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9wyx RCSB], [https://www.ebi.ac.uk/pdbsum/9wyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9wyx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PBSS_PENBI PBSS_PENBI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Terpene synthases (TSs) catalyze the formation of diverse hydrocarbon skeletons by using different linear polyisoprenyl diphosphates as the substrates, whose biosyntheses are catalyzed by prenyltransferases (PTs). In nature, some TSs are bifunctional enzymes catalyzing both polyisoprenyl diphosphate formation and subsequent cyclization, containing a C-terminal PT domain and an N-terminal terpene cyclase (TC) domain. To date, several bifunctional PT-TC diterpene synthases and triterpene synthase have been structurally characterized, whereas there have been no structural insights reported for bifunctional PT-TC sesterterpene synthases (StTSs). We here report the cryo-EM structures of three full-length StTSs (EvAS, EvSS, and PbSS), revealing that EvAS and PbSS share a similar PT-driven hexamerization architecture, but EvSS possesses a PT-hexamer stacked helical hollow tubular architecture that has not been observed for other TSs. Domain swapping among the three StTSs shows that not only the production yields but also the major product types of TCs can be greatly affected by different noncovalently linked PTs. The atypical alpha-helical bundle crystal structure of the TC domain of EvAS was determined, revealing key secondary structures whose positions may affect the cyclization function. Systematic mutations on key residues in the active sites of the TC domains of EvAS and EvSS generated seven new compounds, expanding the structural diversity of sesterterpenes. These results uncover the new structural architecture of bifunctional TSs and expand our understanding of their substrate transfer and catalytic function, and benefit the rational engineering and design of collaborated PT and TC pairs in the generation of terpene molecules.

Structural Insights into Three Bifunctional Sesterterpene Synthases and Product Profile Investigation by Domain Swapping and Active Site Mutation.,Lei Z, Lyu R, Song W, Zhang C, Bai L, Yang D, Ma M J Am Chem Soc. 2026 Jan 23. doi: 10.1021/jacs.5c17651. PMID:41575888<ref>PMID:41575888</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9wyx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Penicillium brasilianum]]
[[Category: Bai L]]
[[Category: Lyu RQ]]