2HMF: Structure Of A Threonine Sensitive Aspartokinase From Methanococcus Jannaschii Complexed With Mg-adp And Aspartate

Citation:
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.
PDB ID: 2HMFDownload
MMDB ID: 42264
PDB Deposition Date: 2006/7/11
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 2HMF: tetrameric; determined by author and by software (PISA)
Molecular Components in 2HMF
Label Count Molecule
Proteins (4 molecules)
4
Probable Aspartokinase(Gene symbol: MJ_RS03010)
Molecule annotation
Chemicals (12 molecules)
1
4
2
4
3
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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