5gul

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:43, 2 August 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of Tris/PPix2/Mg2+ bound form of cyclolavandulyl diphosphate synthase (CLDS) from Streptomyces sp. CL190==
==Crystal structure of Tris/PPix2/Mg2+ bound form of cyclolavandulyl diphosphate synthase (CLDS) from Streptomyces sp. CL190==
-
<StructureSection load='5gul' size='340' side='right' caption='[[5gul]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
+
<StructureSection load='5gul' size='340' side='right'caption='[[5gul]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5gul]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GUL FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5gul]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._CL190 Streptomyces sp. CL190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GUL FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.73&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5guk|5guk]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=5gul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gul OCA], [http://pdbe.org/5gul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gul RCSB], [http://www.ebi.ac.uk/pdbsum/5gul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gul ProSAT]</span></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=5gul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gul OCA], [https://pdbe.org/5gul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gul RCSB], [https://www.ebi.ac.uk/pdbsum/5gul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gul ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/X5IYJ5_STRC1 X5IYJ5_STRC1]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We report the three-dimensional structure of cyclolavandulyl diphosphate (CLPP) synthase (CLDS), which consecutively catalyzes the condensation of two molecules of dimethylallyl diphosphate (DMAPP) followed by cyclization to form a cyclic monoterpene, CLPP. The structures of apo-CLDS and CLDS in complex with Tris, pyrophosphate, and Mg(2+) ion were refined at 2.00 A resolution and 1.73 A resolution, respectively. CLDS adopts a typical fold for cis-prenyl synthases and forms a homo-dimeric structure. An in vitro reaction using a regiospecifically (2) H-substituted DMAPP substrate revealed the intramolecular proton transfer mechanism of the CLDS reaction. The CLDS structure and structure-based mutagenesis provide mechanistic insights into this unprecedented terpene synthase. The combination of structural and mechanistic insights advances the knowledge of intricate terpene synthase-catalyzed reactions.
 +
 +
Structure and Mechanism of the Monoterpene Cyclolavandulyl Diphosphate Synthase that Catalyzes Consecutive Condensation and Cyclization.,Tomita T, Kobayashi M, Karita Y, Yasuno Y, Shinada T, Nishiyama M, Kuzuyama T Angew Chem Int Ed Engl. 2017 Nov 20;56(47):14913-14917. doi:, 10.1002/anie.201708474. Epub 2017 Oct 11. PMID:28922556<ref>PMID:28922556</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5gul" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Kobayashi, M]]
+
[[Category: Large Structures]]
-
[[Category: Kuzuyama, T]]
+
[[Category: Streptomyces sp. CL190]]
-
[[Category: Nishiyama, M]]
+
[[Category: Kobayashi M]]
-
[[Category: Tomita, T]]
+
[[Category: Kuzuyama T]]
-
[[Category: Biosynthetic protein]]
+
[[Category: Nishiyama M]]
-
[[Category: Cis-prenyltransferase]]
+
[[Category: Tomita T]]
-
[[Category: Cyclolavandulyl diphosphate synthase]]
+
-
[[Category: Mg2+]]
+
-
[[Category: Ppi]]
+
-
[[Category: Streptomyces sp. cl190]]
+
-
[[Category: Tri]]
+

Current revision

Crystal structure of Tris/PPix2/Mg2+ bound form of cyclolavandulyl diphosphate synthase (CLDS) from Streptomyces sp. CL190

PDB ID 5gul

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/5gul"
Personal tools