1FJR

CRYSTAL STRUCTURE OF THE ECTODOMAIN OF METHUSELAH

Summary for 1FJR

• Entry DOI: 10.2210/pdb1fjr/pdb
• Descriptor: METHUSELAH ECTODOMAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: gpcr, g protein-coupled receptor, ectodomain, signaling protein
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 47592.46

Authors

West Jr., A.P.,Llamas, L.L.,Snow, P.M.,Benzer, S.,Bjorkman, P.J. (deposition date: 2000-08-08, release date: 2001-04-04, Last modification date: 2024-10-16)

Primary citation

West Jr., A.P.,Llamas, L.L.,Snow, P.M.,Benzer, S.,Bjorkman, P.J.
Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan.
Proc.Natl.Acad.Sci.USA, 98:3744-3749, 2001

PubMed Abstract: The Drosophila mutant methuselah (mth) was identified from a screen for single gene mutations that extended average lifespan. Mth mutants have a 35% increase in average lifespan and increased resistance to several forms of stress, including heat, starvation, and oxidative damage. The protein affected by this mutation is related to G protein-coupled receptors of the secretin receptor family. Mth, like secretin receptor family members, has a large N-terminal ectodomain, which may constitute the ligand binding site. Here we report the 2.3-A resolution crystal structure of the Mth extracellular region, revealing a folding topology in which three primarily beta-structure-containing domains meet to form a shallow interdomain groove containing a solvent-exposed tryptophan that may represent a ligand binding site. The Mth structure is analyzed in relation to predicted Mth homologs and potential ligand binding features.

PubMed: 11274391
DOI: 10.1073/pnas.051625298

Experimental method

X-RAY DIFFRACTION (2.3 Å)