4GO5

The regulatory subunit of aspartate kinase from Mycobacterium tuberculosis

Summary for 4GO5

• Entry DOI: 10.2210/pdb4go5/pdb
• Related: 4GO7
• Descriptor: Aspartokinase (2 entities in total)
• Functional Keywords: transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 21502.20

Authors

Yang, Q.,Li, X. (deposition date: 2012-08-18, release date: 2012-09-05, Last modification date: 2024-02-28)

Primary citation

Yang, Q.,Yu, K.,Yan, L.,Li, Y.,Chen, C.,Li, X.
Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis.
Protein Cell, 2:745-754, 2011

PubMed Abstract: The aspartate kinase (AK) from Mycobacterium tuberculosis (Mtb) catalyzes the biosynthesis of aspartate family amino acids, including lysine, threonine, isoleucine and methionine. We determined the crystal structures of the regulatory subunit of aspartate kinase from Mtb alone (referred to as MtbAKβ) and in complex with threonine (referred to as MtbAKβ-Thr) at resolutions of 2.6 Å and 2.0 Å, respectively. MtbAKβ is composed of two perpendicular non-equivalent ACT domains [aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)] per monomer. Each ACT domain contains two α helices and four antiparallel β strands. The structure of MtbAKβ shares high similarity with the regulatory subunit of the aspartate kinase from Corynebacterium glutamicum (referred to as CgAKβ), suggesting similar regulatory mechanisms. Biochemical assays in our study showed that MtbAK is inhibited by threonine. Based on crystal structure analysis, we discuss the regulatory mechanism of MtbAK.

PubMed: 21976064
DOI: 10.1007/s13238-011-1094-2

Experimental method

X-RAY DIFFRACTION (2.6 Å)