View source for 6lop


==Crystal Structure of Class IB terpene synthase bound with geranylgeraniol==
<StructureSection load='6lop' size='340' side='right'caption='[[6lop]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6lop]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_alcalophilus_ATCC_27647_=_CGMCC_1.3604 Alkalihalobacillus alcalophilus ATCC 27647 = CGMCC 1.3604]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LOP 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]] 1.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELX:(2~{E},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraen-1-ol'>ELX</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=6lop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lop OCA], [https://pdbe.org/6lop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lop RCSB], [https://www.ebi.ac.uk/pdbsum/6lop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lop ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A094YZ24_ALKAL A0A094YZ24_ALKAL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Terpene synthases (TS) are classified into two broad types, Class I and II, based on the chemical strategy for initial carbocation formation and motif sequences of the catalytic site. We have recently identified a new class of enzymes, Class IB, showing the acceptability of long (C20-C35) prenyl-diphosphates as substrates and no amino acid sequence homology with known TS. Conversion of long prenyl-diphosphates such as heptaprenyl-diphosphate (C35) is unusual and has never been reported for Class I and II enzymes. Therefore, the characterization of Class IB enzymes is crucial to understand the reaction mechanism of the extensive terpene synthesis. Here, we report the crystal structure bound with a substrate surrogate and biochemical analysis of a Class IB TS, using the enzyme from Bacillus alcalophilus (BalTS). The structure analysis revealed that the diphosphate part of the substrate is located around the two characteristic Asp-rich motifs, and the hydrophobic tail is accommodated in a unique hydrophobic long tunnel, where the C35 prenyl-diphosphate, the longest substrate of BalTS, can be accepted. Biochemical analyses of BalTS showed that the enzymatic property, such as Mg(2+) dependency, is similar to those of Class I enzymes. In addition, a new cyclic terpene was identified from BalTS reaction products. Mutational analysis revealed that five of the six Asp residues in the Asp-rich motifs and two His residues are essential for the formation of the cyclic skeleton. These results provided a clue to consider the application of the unusual large terpene synthesis by Class IB enzymes.

Characterization of Class IB Terpene Synthase: The First Crystal Structure Bound with a Substrate Surrogate.,Stepanova R, Inagi H, Sugawara K, Asada K, Nishi T, Ueda D, Yasuno Y, Shinada T, Miki K, Fujihashi M, Sato T ACS Chem Biol. 2020 Jun 19;15(6):1517-1525. doi: 10.1021/acschembio.0c00145. Epub, 2020 Apr 13. PMID:32227910<ref>PMID:32227910</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6lop" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Alkalihalobacillus alcalophilus ATCC 27647 = CGMCC 1 3604]]
[[Category: Large Structures]]
[[Category: Fujihashi M]]
[[Category: Inagi H]]
[[Category: Miki K]]