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1ps1

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Revision as of 09:34, 8 September 2021

PENTALENENE SYNTHASE

Structural highlights

1ps1 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Pentalenene synthase, with EC number 4.2.3.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PENA_STREX] Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of pentalenene synthase at 2.6 angstrom resolution reveals critical active site features responsible for the cyclization of farnesyl diphosphate into the tricyclic hydrocarbon pentalenene. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. The core active site structure of the enzyme may be preserved among the greater family of terpenoid synthases, possibly implying divergence from a common ancestral synthase to satisfy biological requirements for increasingly diverse natural products.

Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology.,Lesburg CA, Zhai G, Cane DE, Christianson DW Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cane DE, Sohng JK, Lamberson CR, Rudnicki SM, Wu Z, Lloyd MD, Oliver JS, Hubbard BR. Pentalenene synthase. Purification, molecular cloning, sequencing, and high-level expression in Escherichia coli of a terpenoid cyclase from Streptomyces UC5319. Biochemistry. 1994 May 17;33(19):5846-57. PMID:8180213
↑ Lesburg CA, Zhai G, Cane DE, Christianson DW. Crystal structure of pentalenene synthase: mechanistic insights on terpenoid cyclization reactions in biology. Science. 1997 Sep 19;277(5333):1820-4. PMID:9295272

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ps1"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ps1' size='340' side='right'caption='[[1ps1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ps1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PS1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ps1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PS1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PBM:TRIMETHYL+LEAD+ION'>PBM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PBM:TRIMETHYL+LEAD+ION'>PBM</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pentalenene_synthase Pentalenene synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.7 4.2.3.7] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pentalenene_synthase Pentalenene synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.7 4.2.3.7] </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=1ps1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps1 OCA], [http://pdbe.org/1ps1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ps1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ps1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ps1 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=1ps1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps1 OCA], [https://pdbe.org/1ps1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ps1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ps1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ps1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PENA_STREX PENA_STREX]] Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species.<ref>PMID:8180213</ref>
+[[https://www.uniprot.org/uniprot/PENA_STREX PENA_STREX]] Catalyzes the cyclization of farnesyl diphosphate (FPP) to the tricyclic sesquiterpene pentalenene, which is the hydrocarbon precursor of the pentalenolactone family of antibiotics produced by a variety of Streptomyces species.<ref>PMID:8180213</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ps1

From Proteopedia

Revision as of 09:34, 8 September 2021

PENTALENENE SYNTHASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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