at Google ScholarTitle 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
(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 Jul 2022 11:59 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/10135 |