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.


2c2b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2c2b.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2c2b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c2b| PDB=2c2b | SCENE= }}
{{STRUCTURE_2c2b| PDB=2c2b | SCENE= }}
-
'''CRYSTALLOGRAPHIC STRUCTURE OF ARABIDOPSIS THALIANA THREONINE SYNTHASE COMPLEXED WITH PYRIDOXAL PHOSPHATE AND S-ADENOSYLMETHIONINE'''
+
===CRYSTALLOGRAPHIC STRUCTURE OF ARABIDOPSIS THALIANA THREONINE SYNTHASE COMPLEXED WITH PYRIDOXAL PHOSPHATE AND S-ADENOSYLMETHIONINE===
-
==Overview==
+
<!--
-
Threonine synthase (TS) is a fold-type II pyridoxal phosphate (PLP)-dependent enzyme that catalyzes the ultimate step of threonine synthesis in plants and microorganisms. Unlike the enzyme from microorganisms, plant TS is activated by S-adenosylmethionine (AdoMet). The mechanism of activation has remained unknown up to now. We report here the crystallographic structures of Arabidopsis thaliana TS in complex with PLP (aTS) and with PLP and AdoMet (aTS-AdoMet), which show with atomic detail how AdoMet activates TS. The aTS structure reveals a PLP orientation never previously observed for a type II PLP-dependent enzyme and explains the low activity of plant TS in the absence of its allosteric activator. The aTS-AdoMet structure shows that activation of the enzyme upon AdoMet binding triggers a large reorganization of active site loops in one monomer of the structural dimer and allows the displacement of PLP to its active conformation. Comparison with other TS structures shows that activation of the second monomer may be triggered by substrate binding. This structure also discloses a novel fold for two AdoMet binding sites located at the dimer interface, each site containing two AdoMet effectors bound in tandem. Moreover, aTS-AdoMet is the first structure of an enzyme that uses AdoMet as an allosteric effector.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16319072}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16319072 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16319072}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Synthase]]
[[Category: Synthase]]
[[Category: Threonine synthesis]]
[[Category: Threonine synthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:08:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:11:26 2008''

Revision as of 09:11, 29 July 2008

Image:2c2b.png

Template:STRUCTURE 2c2b

CRYSTALLOGRAPHIC STRUCTURE OF ARABIDOPSIS THALIANA THREONINE SYNTHASE COMPLEXED WITH PYRIDOXAL PHOSPHATE AND S-ADENOSYLMETHIONINE

Template:ABSTRACT PUBMED 16319072

About this Structure

2C2B is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Allosteric threonine synthase. Reorganization of the pyridoxal phosphate site upon asymmetric activation through S-adenosylmethionine binding to a novel site., Mas-Droux C, Biou V, Dumas R, J Biol Chem. 2006 Feb 24;281(8):5188-96. Epub 2005 Nov 29. PMID:16319072

Page seeded by OCA on Tue Jul 29 12:11:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c2b"
Personal tools