3tvi

Crystal structure of Clostridium acetobutylicum aspartate kinase (CaAK): An important allosteric enzyme for industrial amino acids production

spinqualitylabelsall models 3tvi, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tvi is a 12 chain structure with sequence from "clostridium_acetobutyricum"_prevot_1940 "clostridium acetobutyricum" prevot 1940. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ASP, LYS NonStd Res: MSE Gene: CA_C0278 ("Clostridium acetobutyricum" Prevot 1940) Activity: Aspartate kinase, with EC number 2.7.2.4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Aspartate kinase (AK) is an enzyme which is tightly regulated through feedback control and responsible for the synthesis of 4-phospho-L-aspartate from L-aspartate. This intermediate step is at an important branch point where one path leads to the synthesis of lysine and the other to threonine, methionine and isoleucine. Concerted feedback inhibition of AK is mediated by threonine and lysine and varies between the species. The crystal structure of biotechnologically important Clostridium acetobutylicum aspartate kinase (CaAK; E.C. 2.7.2.4; Mw=48,030Da; 437aa; SwissProt: Q97MC0) has been determined to 3A resolution. CaAK acquires a protein fold similar to the other known structures of AKs despite the low sequence identity (<30%). It is composed of two domains: an N-terminal catalytic domain (kinase) domain and a C-terminal regulatory domain further comprised of two small domains belonging to the ACT domain family. Pairwise comparison of 12 molecules in the asymmetric unit helped to identify the bending regions which are in the vicinity of ATP binding site involved in domain movements between the catalytic and regulatory domains. All 12 CaAK molecules adopt fully open T-state conformation leading to the formation of three tetramers unique among other similar AK structures. On the basis of comparative structural analysis, we discuss tetramer formation based on the large conformational changes in the catalytic domain associated with the lysine binding at the regulatory domains. The structure described herein is homologous to a target in wide-spread pathogenic (toxin producing) bacteria such as Clostridium tetani (64% sequence identity) suggesting the potential of the structure solved here to be applied for modeling drug interactions. CaAK structure may serve as a guide to better understand and engineer lysine biosynthesis for the biotechnology industry. Crystal structure of Aspartate kinase (AK): An important allosteric enzyme for amino acids production.,Manjasetty BA, Chance MR, Burley SK, Panjikar S, Almo SC Biotechnol Rep (Amst). 2014 Sep 1;3:73-85. PMID:25170437 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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