View source for 2dtj

[[Image:2dtj.jpg|left|200px]]<br /><applet load="2dtj" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="2dtj, resolution 1.58&Aring;" />
'''Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum'''<br />

==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.

==About this Structure==
2DTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum] with THR and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DTJ 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17350037 17350037]
[[Category: Aspartate kinase]]
[[Category: Corynebacterium glutamicum]]
[[Category: Single protein]]
[[Category: Fushinobu, S.]]
[[Category: Kuzuyama, T.]]
[[Category: Nishiyama, M.]]
[[Category: Tomita, T.]]
[[Category: Yoshida, A.]]
[[Category: CIT]]
[[Category: THR]]
[[Category: protein-ligand complex]]
[[Category: regulatory subunit]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:46:28 2007''