2hmf | pdb_00002hmf
Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate
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Overview
The activation of the beta-carboxyl group of aspartate catalyzed by aspartokinase is the commitment step to amino-acid biosynthesis in the aspartate pathway. The first structure of a microbial aspartokinase, that from Methanococcus jannaschii, has been determined in the presence of the amino-acid substrate L-aspartic acid and the nucleotide product MgADP. The enzyme assembles into a dimer of dimers, with the interfaces mediated by both the N- and C-terminal domains. The active-site functional groups responsible for substrate binding and specificity have been identified and roles have been proposed for putative catalytic functional groups.
About this Structure
2HMF is a Single protein structure of sequence from Methanocaldococcus jannaschii with MG, ADP and ASP as ligands. Active as Aspartate kinase, with EC number 2.7.2.4 Full crystallographic information is available from OCA.
Reference
The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase., Faehnle CR, Liu X, Pavlovsky A, Viola RE, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):962-6. Epub 2006 Sep 30. PMID:17012784
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