6loo
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal Structure of Class IB terpene synthase bound with geranylcitronellyl diphosphate== | ==Crystal Structure of Class IB terpene synthase bound with geranylcitronellyl diphosphate== | ||
| - | <StructureSection load='6loo' size='340' side='right'caption='[[6loo]]' scene=''> | + | <StructureSection load='6loo' size='340' side='right'caption='[[6loo]], [[Resolution|resolution]] 1.99Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LOO OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6loo]] 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=6LOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LOO FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELR:phosphono+[(3~{S},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl]+hydrogen+phosphate'>ELR</scene>, <scene name='pdbligand=ELU:phosphono+[(3~{R},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl]+hydrogen+phosphate'>ELU</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=6loo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6loo OCA], [https://pdbe.org/6loo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6loo RCSB], [https://www.ebi.ac.uk/pdbsum/6loo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6loo ProSAT]</span></td></tr> | ||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6loo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Alkalihalobacillus alcalophilus ATCC 27647 = CGMCC 1 3604]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Fujihashi M]] | [[Category: Fujihashi M]] | ||
[[Category: Inagi H]] | [[Category: Inagi H]] | ||
[[Category: Miki K]] | [[Category: Miki K]] | ||
Current revision
Crystal Structure of Class IB terpene synthase bound with geranylcitronellyl diphosphate
| |||||||||||
