This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3v1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:29, 1 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of 2-methylisoborneol synthase from Streptomyces coelicolor A3(2) in complex with Mg2+ and geranyl-S-thiolodiphosphate==
==Crystal structure of 2-methylisoborneol synthase from Streptomyces coelicolor A3(2) in complex with Mg2+ and geranyl-S-thiolodiphosphate==
-
<StructureSection load='3v1v' size='340' side='right' caption='[[3v1v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='3v1v' size='340' side='right'caption='[[3v1v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3v1v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V1V FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3v1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V1V FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GST:GERANYL+S-THIOLODIPHOSPHATE'>GST</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3v1x|3v1x]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GST:GERANYL+S-THIOLODIPHOSPHATE'>GST</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SC1A4.08, SCBAC12C8.01, SCO7700 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</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=3v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v1v OCA], [https://pdbe.org/3v1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v1v RCSB], [https://www.ebi.ac.uk/pdbsum/3v1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v1v ProSAT]</span></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=3v1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v1v OCA], [http://pdbe.org/3v1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v1v RCSB], [http://www.ebi.ac.uk/pdbsum/3v1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v1v ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/MIBS_STRCO MIBS_STRCO]] Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%).
+
[https://www.uniprot.org/uniprot/MIBS_STRCO MIBS_STRCO] Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%).
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The crystal structure of 2-methylisoborneol synthase (MIBS) from Streptomyces coelicolor A3(2) has been determined in complex with substrate analogues geranyl-S-thiolodiphosphate and 2-fluorogeranyl diphosphate at 1.80 and 1.95 A resolution, respectively. This terpenoid cyclase catalyzes the cyclization of the naturally occurring, noncanonical C-methylated isoprenoid substrate, 2-methylgeranyl diphosphate, to form the bicyclic product 2-methylisoborneol, a volatile C(11) homoterpene alcohol with an earthy, musty odor. While MIBS adopts the tertiary structure of a class I terpenoid cyclase, its dimeric quaternary structure differs from that previously observed in dimeric terpenoid cyclases from plants and fungi. The quaternary structure of MIBS is nonetheless similar in some respects to that of dimeric farnesyl diphosphate synthase, which is not a cyclase. The structures of MIBS complexed with substrate analogues provide insights regarding differences in the catalytic mechanism of MIBS and the mechanisms of (+)-bornyl diphosphate synthase and endo-fenchol synthase, plant cyclases that convert geranyl diphosphate into products with closely related bicyclic bornyl skeletons, but distinct structures and stereochemistries.
+
-
 
+
-
Structure of 2-Methylisoborneol Synthase from Streptomyces coelicolor and Implications for the Cyclization of a Noncanonical C-Methylated Monoterpenoid Substrate.,Koksal M, Chou WK, Cane DE, Christianson DW Biochemistry. 2012 Apr 10;51(14):3011-20. Epub 2012 Mar 28. PMID:22455514<ref>PMID:22455514</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3v1v" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Strco]]
+
[[Category: Large Structures]]
-
[[Category: Christianson, D W]]
+
[[Category: Christianson DW]]
-
[[Category: Koksal, M]]
+
[[Category: Koksal M]]
-
[[Category: 2-methylisoborneol biosynthesis]]
+
-
[[Category: Biosynthesis of 2-methylisoborneol]]
+
-
[[Category: Class i terpenoid cyclase fold]]
+
-
[[Category: Ddxxxxd motif]]
+
-
[[Category: Lyase]]
+
-
[[Category: Ndxxsxxxe motif]]
+

Current revision

Crystal structure of 2-methylisoborneol synthase from Streptomyces coelicolor A3(2) in complex with Mg2+ and geranyl-S-thiolodiphosphate

PDB ID 3v1v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3v1v"
Personal tools