2HMF

Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate

Summary for 2HMF

Entry DOI	10.2210/pdb2hmf/pdb
Related	2CDQ
Descriptor	Probable aspartokinase, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywords	aspartokinase, transferase
Biological source	Methanocaldococcus jannaschii
Total number of polymer chains	4
Total formula weight	206433.04
Authors	Faehnle, C.R.,Viola, R.E. (deposition date: 2006-07-11, release date: 2006-10-17, Last modification date: 2023-08-30)
Primary citation	Faehnle, C.R.,Liu, X.,Pavlovsky, A.,Viola, R.E. The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase. Acta Crystallogr.,Sect.F, 62:962-966, 2006 Cited by PubMed Abstract: 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. PubMed: 17012784 DOI: 10.1107/S1744309106038279 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation