3cke

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3cke.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3cke.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3cke| PDB=3cke | SCENE= }}
{{STRUCTURE_3cke| PDB=3cke | SCENE= }}
-
'''Crystal structure of aristolochene synthase in complex with 12,13-difluorofarnesyl diphosphate'''
+
===Crystal structure of aristolochene synthase in complex with 12,13-difluorofarnesyl diphosphate===
-
==Overview==
+
<!--
-
The universal sesquiterpene precursor, farnesyl diphosphate (FPP), is cyclized in an Mg(2+)-dependent reaction catalyzed by the tetrameric aristolochene synthase from Aspergillus terreus to form the bicyclic hydrocarbon aristolochene and a pyrophosphate anion (PP(i)) coproduct. The 2.1-A resolution crystal structure determined from crystals soaked with FPP reveals the binding of intact FPP to monomers A-C, and the binding of PP(i) and Mg(2+)(B) to monomer D. The 1.89-A resolution structure of the complex with 2-fluorofarnesyl diphosphate (2F-FPP) reveals 2F-FPP binding to all subunits of the tetramer, with Mg(2+)(B)accompanying the binding of this analogue only in monomer D. All monomers adopt open activesite conformations in these complexes, but slight structural changes in monomers C and D of each complex reflect the very initial stages of a conformational transition to the closed state. Finally, the 2.4-A resolution structure of the complex with 12,13-difluorofarnesyl diphosphate (DF-FPP) reveals the binding of intact DF-FPP to monomers A-C in the open conformation and the binding of PP(i), Mg(2+)(B), and Mg(2+)(C) to monomer D in a predominantly closed conformation. Taken together, these structures provide 12 independent "snapshots" of substrate or product complexes that suggest a possible sequence for metal ion binding and conformational changes required for catalysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18385128}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18385128 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18385128}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Metal ion binding]]
[[Category: Metal ion binding]]
[[Category: Substrate binding]]
[[Category: Substrate binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:21:52 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:31:28 2008''

Revision as of 14:31, 27 July 2008

Image:3cke.png

Template:STRUCTURE 3cke

Crystal structure of aristolochene synthase in complex with 12,13-difluorofarnesyl diphosphate

Template:ABSTRACT PUBMED 18385128

About this Structure

3CKE is a Single protein structure of sequence from Aspergillus terreus. Full crystallographic information is available from OCA.

Reference

X-ray Crystallographic Studies of Substrate Binding to Aristolochene Synthase Suggest a Metal Ion Binding Sequence for Catalysis., Shishova EY, Yu F, Miller DJ, Faraldos JA, Zhao Y, Coates RM, Allemann RK, Cane DE, Christianson DW, J Biol Chem. 2008 May 30;283(22):15431-9. Epub 2008 Apr 2. PMID:18385128

Page seeded by OCA on Sun Jul 27 17:31:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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