1PM3

MTH1859

Summary for 1PM3

• Entry DOI: 10.2210/pdb1pm3/pdb
• Descriptor: MTH1895 (1 entity in total)
• Functional Keywords: unknown function, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 2
• Total formula weight: 20846.03

Authors

Ye, H.,Steegborn, C.,Wu, H.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2003-06-09, release date: 2003-08-12, Last modification date: 2024-02-14)

Primary citation

Ye, H.,Chen, T.C.,Xu, X.,Pennycooke, M.,Wu, H.,Steegborn, C.
Crystal structure of the putative adapter protein MTH1859.
J.Struct.Biol., 148:251-256, 2004

PubMed Abstract: MTH1859 from Methanobacterium thermoautotrophicum is a 77 residue protein representing a conserved family of functionally uncharacterized proteins. We solved the crystal structure of MTH1859 by single wavelength anomalous diffraction phasing using selenomethionine labeled protein. MTH1859 adopts a mainly anti-parallel all-beta-fold. The beta-sheet is heavily bent to form a U-structure that is closed through a loop. The monomer structure possesses similarities to the photoreaction center (PRC) domain fold, but the protein employs a unique oligomerization scheme. Two monomers of MTH1859 occupy the asymmetric unit and dimerize in a head-to-head fashion. Crystal packing interactions identify a second protein-protein interaction interface at the MTH1859 tails which can simultaneously bind two partner molecules. These interactions lead to the formation of a honeycomb structure and suggest that the family of MTH1859-like proteins might function as adapters for protein complex assembly.

PubMed: 15477104
DOI: 10.1016/j.jsb.2004.06.004

Experimental method

X-RAY DIFFRACTION (3.15 Å)