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Crystal structure of the putative adapter protein MTH1859.

Title data

Ye, Hong ; Chen, Tzu-Chao ; Xu, Xiaohui ; Pennycooke, Micha ; Wu, Hao ; Steegborn, Clemens:
Crystal structure of the putative adapter protein MTH1859.
In: Journal of Structural Biology. Vol. 148 (November 2004) Issue 2 . - pp. 251-256.
ISSN 1047-8477
DOI: https://doi.org/10.1016/j.jsb.2004.06.004

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 15477104
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 14 Apr 2015 10:08
Last Modified: 14 Apr 2015 10:08
URI: https://eref.uni-bayreuth.de/id/eprint/10135