3AB4
Crystal structure of feedback inhibition resistant mutant of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine
Summary for 3AB4
| Entry DOI | 10.2210/pdb3ab4/pdb |
| Related | 2DTJ 3AAW 3AB2 |
| Descriptor | Aspartokinase, THREONINE, LYSINE, ... (5 entities in total) |
| Functional Keywords | aspartate kinase, concerted inhibition, alternative initiation, amino-acid biosynthesis, atp-binding, diaminopimelate biosynthesis, kinase, lysine biosynthesis, nucleotide-binding, transferase |
| Biological source | Corynebacterium glutamicum (Brevibacterium flavum) More |
| Total number of polymer chains | 16 |
| Total formula weight | 517364.02 |
| Authors | Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2009-11-30, release date: 2010-06-23, Last modification date: 2023-11-01) |
| Primary citation | Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. Mechanism of concerted inhibition of {alpha}2{beta}2-type heterooligomeric aspartate kinase from Corynebacterium glutamicum J.Biol.Chem., 285:27477-27486, 2010 Cited by PubMed Abstract: Aspartate kinase (AK) is the first and committed enzyme of the biosynthetic pathway producing aspartate family amino acids, lysine, threonine, and methionine. AK from Corynebacterium glutamicum (CgAK), a bacterium used for industrial fermentation of amino acids, including glutamate and lysine, is inhibited by lysine and threonine in a concerted manner. To elucidate the mechanism of this unique regulation in CgAK, we determined the crystal structures in several forms: an inhibitory form complexed with both lysine and threonine, an active form complexed with only threonine, and a feedback inhibition-resistant mutant (S301F) complexed with both lysine and threonine. CgAK has a characteristic alpha(2)beta(2)-type heterotetrameric structure made up of two alpha subunits and two beta subunits. Comparison of the crystal structures between inhibitory and active forms revealed that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit (regulatory subunit) is a key event for stabilizing the inhibitory form. This study shows not only the first crystal structures of alpha(2)beta(2)-type AK but also the mechanism of concerted inhibition in CgAK. PubMed: 20573952DOI: 10.1074/jbc.M110.111153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.47 Å) |
Structure validation
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