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 protein domain family PF12095 (DUF3571) is a functionally uncharacterized family of small proteins conserved from cyanobacteria to plants that are typically 85 to 95 amino acids in length in cyanobacteria. In this report, we describe the solution NMR structure of the 86-residue protein Asl3597 from Nostoc sp. PCC7120. The structure of Asl3597, which constitutes the first three-dimensional structure from protein family PF12095, has a unique alpha/beta sandwich fold consisting of four anti-parallel beta-strands opposite three continuous alpha-helices. Asl3597 may have a role in the assembly of the hydrophilic subcomplex of the cyanobacterial NAD(P)H complex as suggested by data for the orthologous Chlororespiratory reduction 7 protein from Arabidopsis thaliana.
Solution NMR structure of Asl3597 from Nostoc sp. PCC7120, the first structure from protein domain family PF12095, reveals a novel fold.,Feldmann EA, Ramelot TA, Yang Y, Xiao R, Acton TB, Everett JK, Montelione GT, Kennedy MA Proteins. 2012 Feb;80(2):671-5. doi: 10.1002/prot.23236. Epub 2011 Nov 24. PMID:22113821[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feldmann EA, Ramelot TA, Yang Y, Xiao R, Acton TB, Everett JK, Montelione GT, Kennedy MA. Solution NMR structure of Asl3597 from Nostoc sp. PCC7120, the first structure from protein domain family PF12095, reveals a novel fold. Proteins. 2011 Oct 29. doi: 10.1002/prot.23236. PMID:22113821 doi:10.1002/prot.23236
