2cdq
Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionineCrystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine
Structural highlights
FunctionAK1_ARATH Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAsp kinase catalyzes the first step of the Asp-derived essential amino acid pathway in plants and microorganisms. Depending on the source organism, this enzyme contains up to four regulatory ACT domains and exhibits several isoforms under the control of a great variety of allosteric effectors. We report here the dimeric structure of a Lys and S-adenosylmethionine-sensitive Asp kinase isoform from Arabidopsis thaliana in complex with its two inhibitors. This work reveals the structure of an Asp kinase and an enzyme containing two ACT domains cocrystallized with its effectors. Only one ACT domain (ACT1) is implicated in effector binding. A loop involved in the binding of Lys and S-adenosylmethionine provides an explanation for the synergistic inhibition by these effectors. The presence of S-adenosylmethionine in the regulatory domain indicates that ACT domains are also able to bind nucleotides. The organization of ACT domains in the present structure is different from that observed in Thr deaminase and in the regulatory subunit of acetohydroxyacid synthase III. A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase.,Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R Plant Cell. 2006 Jul;18(7):1681-92. Epub 2006 May 26. PMID:16731588[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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