1pm3

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pm3 OCA], [https://pdbe.org/1pm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pm3 RCSB], [https://www.ebi.ac.uk/pdbsum/1pm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pm3 ProSAT], [https://www.topsan.org/Proteins/NESGC/1pm3 TOPSAN]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15477104</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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