1jfa: Difference between revisions

Revision as of 20:09, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jfa.png

Template:STRUCTURE 1jfa

TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDESTRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES

Template:ABSTRACT PUBMED 11698643

About this StructureAbout this Structure

1JFA is a Single protein structure of sequence from Fusarium sporotrichioides. Full crystallographic information is available from OCA.

ReferenceReference

Structure of trichodiene synthase from Fusarium sporotrichioides provides mechanistic inferences on the terpene cyclization cascade., Rynkiewicz MJ, Cane DE, Christianson DW, Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13543-8. Epub 2001 Nov 6. PMID:11698643

Page seeded by OCA on Tue Jul 1 20:09:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jfa.jpg|left|200px]]
+{{Seed}}
+[[Image:1jfa.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jfa|  PDB=1jfa  |  SCENE=  }}
-'''TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES'''
+===TRICHODIENE SYNTHASE FROM FUSARIUM SPOROTRICHIOIDES===
-==Overview==
+<!--
-The x-ray crystal structure of recombinant trichodiene synthase from Fusarium sporotrichioides has been determined to 2.5-A resolution, both unliganded and complexed with inorganic pyrophosphate. This reaction product coordinates to three Mg(2+) ions near the mouth of the active site cleft. A comparison of the liganded and unliganded structures reveals a ligand-induced conformational change that closes the mouth of the active site cleft. Binding of the substrate farnesyl diphosphate similarly may trigger this conformational change, which would facilitate catalysis by protecting reactive carbocationic intermediates in the cyclization cascade. Trichodiene synthase also shares significant structural similarity with other sesquiterpene synthases despite a lack of significant sequence identity. This similarity indicates divergence from a common ancestor early in the evolution of terpene biosynthesis.
+The line below this paragraph, {{ABSTRACT_PUBMED_11698643}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11698643 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11698643}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Rynkiewicz, M J.]]
 [[Category: Terpenoid synthase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:09:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:09:35 2008''