Structural highlights
Function
[Q9KUU1_VIBCH] Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome (By similarity).[HAMAP-Rule:MF_01888]
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 structure of Vibrio cholerae protein VC0424 was determined by NMR spectroscopy. VC0424 belongs to a conserved family of bacterial proteins of unknown function (COG 3076). The structure has an alpha-beta sandwich architecture consisting of two layers: a four-stranded antiparallel beta-sheet and three side-by-side alpha-helices. The secondary structure elements have the order alphabetaalphabetabetaalphabeta along the sequence. This fold is the same as the ferredoxin-like fold, except with an additional long N-terminal helix, making it a variation on this common motif. A cluster of conserved surface residues on the beta-sheet side of the protein forms a pocket that may be important for the biological function of this conserved family of proteins.
Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold.,Ramelot TA, Ni S, Goldsmith-Fischman S, Cort JR, Honig B, Kennedy MA Protein Sci. 2003 Jul;12(7):1556-61. PMID:12824501[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ramelot TA, Ni S, Goldsmith-Fischman S, Cort JR, Honig B, Kennedy MA. Solution structure of Vibrio cholerae protein VC0424: a variation of the ferredoxin-like fold. Protein Sci. 2003 Jul;12(7):1556-61. PMID:12824501
