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.


3c20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_3c20", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:3c20.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3c20.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3c20| PDB=3c20 | SCENE= }}
{{STRUCTURE_3c20| PDB=3c20 | SCENE= }}
-
'''Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate'''
+
===Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate===
-
==Overview==
+
<!--
-
The commitment step to the aspartate pathway of amino acid biosynthesis is the phosphorylation of aspartic acid catalyzed by aspartokinase (AK). Most microorganisms and plants have multiple forms of this enzyme, and many of these isofunctional enzymes are subject to feedback regulation by the end products of the pathway. However, the archeal species M. jannaschii has only a single, monofunctional form of AK. The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK (Angeles et al., Biochemistry 31, 799, 1992). Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. In contrast, the highly cooperative binding of the allosteric regulator L-threonine to multiple sites on this dimer of dimers leads to a more open enzyme structure. A comparison of these structures supports a mechanism for allosteric regulation of AK in which the domain movements induced by threonine binding causes displacement of the substrates from the enzyme resulting in a relaxed, inactive conformation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18334478}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18334478 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18334478}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Threonine biosynthesis]]
[[Category: Threonine biosynthesis]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:35:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:13:15 2008''

Revision as of 19:13, 28 July 2008

Image:3c20.png

Template:STRUCTURE 3c20

Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate

Template:ABSTRACT PUBMED 18334478

About this Structure

3C20 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

The structural basis for allosteric Inhibition of a threonine-sensitive aspartokinase., Liu X, Pavlovsky AG, Viola RE, J Biol Chem. 2008 Mar 11;. PMID:18334478

Page seeded by OCA on Mon Jul 28 22:13:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3c20"
Personal tools