3LFZ

Crystal Structure of Protein MJ1225 from Methanocaldococcus jannaschii, a putative archaeal homolog of g-AMPK.

Summary for 3LFZ

• Entry DOI: 10.2210/pdb3lfz/pdb
• Related: 3KH5
• Descriptor: protein MJ1225, ADENOSINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: mj1225, ampk, amp, adp, cbs domain, archaea, methanocaldococcus jannaschii, unknown function
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 1
• Total formula weight: 33550.67

Authors

Gomez-Garcia, I.,Oyenarte, I.,Kortazar, D.,Martinez-Cruz, L.A. (deposition date: 2010-01-19, release date: 2010-04-21, Last modification date: 2023-09-06)

Primary citation

Gomez-Garcia, I.,Oyenarte, I.,Martinez-Cruz, L.A.
The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPK.
J.Mol.Biol., 65:813-817, 2010

PubMed Abstract: In mammals, 5'-AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma-subunit senses the intracellular energy status by competitively binding AMP and ATP and is thought to be responsible for allosteric regulation of the whole complex. We describe herein the crystal structure of protein MJ1225 from Methanocaldococcus jannaschii complexed to AMP, ADP, and ATP. Our data provide evidence of a strong conservation of the key functional features seen in the gamma-subunit of the eukaryotic AMPK, and more importantly, it reveals a novel AMP binding site, herein denoted as site E, which had not been previously described in cystathionine beta-synthase domains so far. Site E is located in a small cavity existing between the alpha-helices structurally equivalent to those disrupting the internal symmetry of each Bateman domain in gamma-AMPKs and shows striking similarities with a symmetry-related crevice of the mammalian enzyme that hosts the pathological mutation N488I.

PubMed: 20382158
DOI: 10.1016/j.jmb.2010.03.045

Experimental method

X-RAY DIFFRACTION (2.2 Å)