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

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)