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.


2dtj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2dtj.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2dtj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2dtj| PDB=2dtj | SCENE= }}
{{STRUCTURE_2dtj| PDB=2dtj | SCENE= }}
-
'''Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum'''
+
===Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum===
-
==Overview==
+
<!--
-
Aspartate kinase (AK) catalyzes the first step of the biosynthesis of the aspartic acid family amino acids, and is regulated via feedback inhibition by end-products including Thr and Lys. To elucidate the mechanism of this inhibition, we determined the crystal structure of the regulatory subunit of AK from Corynebacterium glutamicum at 1.58 A resolution in the Thr-binding form, the first crystal structure of the regulatory subunit of alpha(2)beta(2)-type AK. The regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer. Two non-equivalent ACT domains from different chains form an effector-binding unit that binds a single Thr molecule, and the resulting two effector-binding units of the dimer associate perpendicularly in a face-to-face manner. The regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr. The dimerization is eliminated in mutant AKs with changes in the Thr-binding region, suggesting that the dimerization induced by Thr binding is a key step in the inhibitory mechanism of AK from C. glutamicum. A putative Lys-binding site and the inhibitory mechanism of CgAK are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17350037}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17350037 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17350037}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum., Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M, J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17350037 17350037]
Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum., Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M, J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17350037 17350037]
 +
 +
Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase., Thierbach G, Kalinowski J, Bachmann B, Puhler A, Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1366393 1366393]
 +
 +
Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum., Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A, Mol Microbiol. 1991 May;5(5):1197-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1956296 1956296]
 +
 +
Conversion of feedback regulation in aspartate kinase by domain exchange., Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M, Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15033471 15033471]
[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
Line 30: Line 40:
[[Category: Protein-ligand complex]]
[[Category: Protein-ligand complex]]
[[Category: Regulatory subunit]]
[[Category: Regulatory subunit]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:21:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:51:07 2008''

Revision as of 15:51, 27 July 2008

Image:2dtj.png

Template:STRUCTURE 2dtj

Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum

Template:ABSTRACT PUBMED 17350037

About this Structure

2DTJ is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

Reference

Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum., Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M, J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:17350037

Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase., Thierbach G, Kalinowski J, Bachmann B, Puhler A, Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:1366393

Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum., Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A, Mol Microbiol. 1991 May;5(5):1197-204. PMID:1956296

Conversion of feedback regulation in aspartate kinase by domain exchange., Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M, Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:15033471

Page seeded by OCA on Sun Jul 27 18:51:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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