1DUS

MJ0882-A hypothetical protein from M. jannaschii

Summary for 1DUS

• Entry DOI: 10.2210/pdb1dus/pdb
• Descriptor: MJ0882 (2 entities in total)
• Functional Keywords: hypothetical protein, methanococcus jannaschii, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 1
• Total formula weight: 21945.17

Authors

Hung, L.,Huang, L.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2000-01-18, release date: 2000-07-19, Last modification date: 2011-07-13)

Primary citation

Huang, L.,Hung, L.,Odell, M.,Yokota, H.,Kim, R.,Kim, S.H.
Structure-based experimental confirmation of biochemical function to a methyltransferase, MJ0882, from hyperthermophile Methanococcus jannaschii
J.STRUCT.FUNCT.GENOM., 2:121-127, 2002

PubMed Abstract: We have determined the three-dimensional (3-D) structure of protein MJ0882, which derives from a hypothetical open reading frame in the genome of the hyperthermophile Methanococcus jannaschii. The 3-D fold of MJ0882 at 1.8 A highly resembles that of a methyltransferase, despite limited sequence similarity to any confirmed methyltransferase. The structure has an S-adenosylmethionine (AdoMet) binding pocket surrounded by motifs with similarities to those commonly found among AdoMet binding proteins. Preliminary biochemical experiments show that MJ0882 specifically binds to AdoMet, which is the essential co-factor for methyltransferases.

PubMed: 12836702
DOI: 10.1023/A:1021279113558

Experimental method

X-RAY DIFFRACTION (1.8 Å)