1pm3
From Proteopedia
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'''MTH1859''' | '''MTH1859''' | ||
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| - | [[Category: | + | [[Category: Northeast structural genomics consortium]] |
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Revision as of 02:14, 3 May 2008
MTH1859
Overview
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.
About this Structure
1PM3 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the putative adapter protein MTH1859., Ye H, Chen TC, Xu X, Pennycooke M, Wu H, Steegborn C, J Struct Biol. 2004 Nov;148(2):251-6. PMID:15477104 Page seeded by OCA on Sat May 3 05:14:23 2008
