Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The stand-alone RAM (regulation of amino-acid metabolism) domain protein SraA from Thermus thermophilus HB8 (TTHA0845) was crystallized in the presence of zinc ions. The X-ray crystal structure was determined using a multiple-wavelength anomalous dispersion technique and was refined at 2.4 A resolution to a final R factor of 25.0%. The monomeric structure is a betaalphabetabetaalphabeta fold and it dimerizes mainly through interactions between the antiparallel beta-sheets. Furthermore, five SraA dimers form a ring with external and internal diameters of 70 and 20 A, respectively. This decameric structure is unique compared with the octameric and dodecameric structures found for other stand-alone RAM-domain proteins and the C-terminal RAM domains of Lrp/AsnC-family proteins.
Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8.,Nakano N, Okazaki N, Satoh S, Takio K, Kuramitsu S, Shinkai A, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):855-60. Epub 2006 Aug 26. PMID:16946463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nakano N, Okazaki N, Satoh S, Takio K, Kuramitsu S, Shinkai A, Yokoyama S. Structure of the stand-alone RAM-domain protein from Thermus thermophilus HB8. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):855-60. Epub 2006 Aug 26. PMID:16946463 doi:10.1107/S1744309106031150
