PDBsum entry 3lfz

Unknown function

PDB id: 3lfz

Contents

Protein chain

280 a.a. *

Ligands

ATP ×2

ADP

AMP

Waters ×16

* Residue conservation analysis

PDB id:

3lfz

Name:

Unknown function

Title:

Crystal structure of protein mj1225 from methanocaldococcus jannaschii, a putative archaeal homolog of g-ampk.

Structure:

Protein mj1225. Chain: a. Engineered: yes

Source:

Methanocaldococcus jannaschii. Organism_taxid: 2190. Gene: mj1225. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.20Å R-factor: 0.253 R-free: 0.285

Authors:

I.Gomez-Garcia,I.Oyenarte,D.Kortazar,L.A.Martinez-Cruz

Key ref:

I.Gómez-García et al. (2010). 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, 399, 53-70. PubMed id: 20382158

Date:

19-Jan-10 Release date: 21-Apr-10

Protein chain

Q58622  (Y1225_METJA) -  Uncharacterized protein MJ1225 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

Seq: 280 a.a.

Struc: 280 a.a.

Enzyme reactions

• Enzyme class: E.C.?

J Mol Biol 399:53-70 (2010)

PubMed id: 20382158

The crystal structure of protein MJ1225 from Methanocaldococcus jannaschii shows strong conservation of key structural features seen in the eukaryal gamma-AMPK.

I.Gómez-García, I.Oyenarte, L.A.Martínez-Cruz.

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.