Strictosidine Synthase: Difference between revisions

From Proteopedia
Jump to navigationJump to search
New page: <applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" /> ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol a...
 
Michal Harel (talk | contribs)
No edit summary
 
(30 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<applet load="2fp8" size="300" color="white" frame="true" align="right" spinBox="true" />
<StructureSection load='2fpb' size='350' side='right' caption='Strictosidine synthase dimer complex with tryptamine (PDB entry [[2fpb]])' scene='10/100149/Cv/3'>


==This is a placeholder==
This is a placeholder text to help you get started in
placing a Jmol applet on your page. At any time, click
"Show Preview" at the bottom of this page to see how it goes.


Replace the PDB id after the load=" to load and display
== Function ==
another structure.
The enzyme '''strictosidine synthase''' (<scene name='Strictisidine_Synthase/Str1_sp/1'>STR1</scene>) (EC 4.3.3.2) from an Indian medicinal plant ''Rauvolfia serpentina'' is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ~2000 compounds in higher plants. The enzyme is involved in the biosynthesis of all these alkaloids by catalyzing the condensation of the two initial building blocks, tryptamine and the monoterpenoid secologanin, leading to the glucoalkaloid strictosidine. The reaction type catalyzed by STR1 is so far an exceptional example in the biosynthesis of natural products. It was hitherto known only from synthetic chemistry (Pictet-Spengler–type reaction), where it is applied in alkaloid synthesis, especially of tetrahydroisoquinolines by condensation of an amine and an aldehyde under acidic conditions<ref>PMID:18280746</ref>.
 
The overall structure of the enzyme contains a six-bladed four-stranded ß-propeller fold. All six blades are radially arranged around a pseudo six-fold symmetry axis. Each blade contains a twisted four-stranded antiparallel ß-sheet.
 
== Structural highlights ==
The <scene name='10/100149/Cv/8'>substrate binding pocket of STR1 is located near the pseudo six-fold symmetry axis</scene><ref>PMID:16531499</ref>. {{Template:ColorKey_Helix}},
{{Template:ColorKey_Strand}},
{{Template:ColorKey_Loop}},
{{Template:ColorKey_Turn}}. <scene name='10/100149/Cv/9'>Active site</scene>. Water molecule are shown as red sphere.
</StructureSection>
==3D structures of strictosidine synthase==
 
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
[[2fp8]] – sSTR1 – serpentwood<br />
[[3v1s]] – dSTR - devilpepper<br />
[[2fp9]] – sSTR1 + tartaric acid
 
[[2fpb]] – sSTR1 (mutant) + tryptamine
 
[[2fpc]] – sSTR1 + secologanin
 
[[2v91]] – sSTR1 residues 32-333 + strictosidine
 
[[2vaq]] – sSTR1 + inhibitor<br />
[[6n5v]], [[7t5i]], [[7t5j]] – sSTR + indole derivative <br />
[[4imb]], [[4iyg]] – dSTR + indole derivative <br />
[[6s5q]], [[6s5u]], [[6s5j]], [[6s5m]] – STR + carboline derivative – ''Ophiorrhiza pumila''<br />
[[6zea]] – STR + carboline derivative – periwinkle<br />
== References ==
<references/>
[[Category: Topic Page]]

Latest revision as of 08:46, 6 December 2023

Strictosidine synthase dimer complex with tryptamine (PDB entry 2fpb)

Drag the structure with the mouse to rotate

3D structures of strictosidine synthase

Updated on 06-December-2023

2fp8 – sSTR1 – serpentwood
3v1s – dSTR - devilpepper
2fp9 – sSTR1 + tartaric acid

2fpb – sSTR1 (mutant) + tryptamine

2fpc – sSTR1 + secologanin

2v91 – sSTR1 residues 32-333 + strictosidine

2vaq – sSTR1 + inhibitor
6n5v, 7t5i, 7t5j – sSTR + indole derivative
4imb, 4iyg – dSTR + indole derivative
6s5q, 6s5u, 6s5j, 6s5m – STR + carboline derivative – Ophiorrhiza pumila
6zea – STR + carboline derivative – periwinkle

References

Proteopedia Page Contributors and Editors (what is this?)

Santosh Panjikar, Michal Harel, Alexander Berchansky