This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1kiz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kiz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kiz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kiz| PDB=1kiz | SCENE= }}
{{STRUCTURE_1kiz| PDB=1kiz | SCENE= }}
-
'''D100E trichodiene synthase complexed with pyrophosphate'''
+
===D100E trichodiene synthase complexed with pyrophosphate===
-
==Overview==
+
<!--
-
The 2.4 A resolution X-ray crystal structure of D100E trichodiene synthase and the 2.6 A resolution structure of its complex with inorganic pyrophosphate are reported. The D100E amino acid substitution in the so-called "aspartate-rich" motif does not result in large changes to the overall structure of the enzyme. In the pyrophosphate complex, however, pyrophosphate coordinates two Mg(2+) ions at the mouth of the active site without causing large changes in the structure of the enzyme. This contrasts with pyrophosphate binding in the wild-type enzyme, where pyrophosphate coordinates three Mg(2+) ions and triggers a significant conformational change that closes the mouth of the active site and optimizes packing density in the enzyme-substrate complex. The attenuation of active site closure in D100E trichodiene synthase compromises enzyme-substrate packing density and confers additional spatial and conformational degrees of freedom on the substrate and carbocation intermediates, which in turn results in the formation of five alternate sesquiterpene products in addition to trichodiene. By extension, then, the diversity of terpene cyclases in biology may have evolved in part by amino acid substitutions that fine-tune structural changes dependent on metal-diphosphate complexation that govern the formation of the active site template and enzyme-substrate packing density.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11827517}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11827517 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11827517}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Site-directed mutant]]
[[Category: Site-directed mutant]]
[[Category: Terpenoid synthase fold]]
[[Category: Terpenoid synthase fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:48:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:24:58 2008''

Revision as of 07:24, 2 July 2008

Image:1kiz.png

Template:STRUCTURE 1kiz

D100E trichodiene synthase complexed with pyrophosphate

Template:ABSTRACT PUBMED 11827517

About this Structure

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

Reference

X-ray crystal structures of D100E trichodiene synthase and its pyrophosphate complex reveal the basis for terpene product diversity., Rynkiewicz MJ, Cane DE, Christianson DW, Biochemistry. 2002 Feb 12;41(6):1732-41. PMID:11827517

Page seeded by OCA on Wed Jul 2 10:24:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kiz"
Personal tools