4mc8: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Hedycaryol synthase in complex with HEPES== | |||
=== | <StructureSection load='4mc8' size='340' side='right' caption='[[4mc8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mc8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Kitsk Kitsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MC8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MC8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hm4|1hm4]], [[4mc0|4mc0]], [[4mc3|4mc3]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KSE_00200t, KSE_76540t ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=452652 KITSK])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mc8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mc8 RCSB], [http://www.ebi.ac.uk/pdbsum/4mc8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The biosynthesis of terpenes is catalysed by class I and II terpene cyclases. Here we present structural data from a class I hedycaryol synthase in complex with nerolidol, serving as a surrogate for the reaction intermediate nerolidyl diphosphate. This prefolded ligand allows mapping of the active site and hence the identification of a key carbonyl oxygen of Val179, a highly conserved helix break (G1/2) and its corresponding helix dipole. Stabilising the carbocation at the substrate's C1 position, these elements act in concert to catalyse the 1,10 ring closure, thereby exclusively generating the anti-Markovnikov product. The delineation of a general mechanistic scaffold was confirmed by site-specific mutations. This work serves as a basis for understanding carbocation chemistry in enzymatic reactions and should contribute to future application of these enzymes in organic synthesis. | |||
Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism.,Baer P, Rabe P, Citron CA, de Oliveira Mann CC, Kaufmann N, Groll M, Dickschat JS Chembiochem. 2014 Jan 24;15(2):213-6. doi: 10.1002/cbic.201300708. Epub 2014 Jan , 7. PMID:24399794<ref>PMID:24399794</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Baer, P | == References == | ||
[[Category: Cirton, C | <references/> | ||
[[Category: Dickschat, J | __TOC__ | ||
[[Category: Groll, M | </StructureSection> | ||
[[Category: Kaufmann, N | [[Category: Kitsk]] | ||
[[Category: Mann, C Oliveira | [[Category: Baer, P]] | ||
[[Category: Rabe, P | [[Category: Cirton, C]] | ||
[[Category: Dickschat, J]] | |||
[[Category: Groll, M]] | |||
[[Category: Kaufmann, N]] | |||
[[Category: Mann, C Oliveira]] | |||
[[Category: Rabe, P]] | |||
[[Category: Cyclase]] | [[Category: Cyclase]] | ||
[[Category: Helix break]] | [[Category: Helix break]] | ||
Revision as of 09:04, 5 January 2015
Hedycaryol synthase in complex with HEPES
| ||||||||||||
