Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
YgfZ, beta-barrel domain
YgfZ is a folate-binding protein involved in regulating the level of ATP-dnaA and in the modification of some tRNAs [1,2]. It consists of a folate-binding domain at the N-terminal (Pfam:PF01571) and a six-stranded antiparallel beta-barrel at the C-terminal, represented in this entry, with identical topology found at the C-terminal of elongation factors Tu and eEF-1alpha and in the gamma subunit of the initiation factor eIF2 [1]. Paper describing PDB structure 1nrk. [1]. 15489424. Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolism. Teplyakov A, Obmolova G, Sarikaya E, Pullalarevu S, Krajewski W, Galkin A, Howard AJ, Herzberg O, Gilliland GL;. J Bacteriol. 2004;186:7134-7140. [2]. 16359333. Involvement of the Escherichia coli folate-binding protein YgfZ in RNA modification and regulation of chromosomal replication initiation. Ote T, Hashimoto M, Ikeuchi Y, Su'etsugu M, Suzuki T, Katayama T, Kato J;. Mol Microbiol. 2006;59:265-275. (from Pfam)
folate-binding protein YgfZ
YgfZ is a protein from Escherichia coli, homologous to the glycine cleavage system T protein, or aminomethyltransferase, GcvT (TIGR00528). Homologs of YgfZ other than members of the GcvT family share a well-conserved signature region that includes the motif, KGCYxGQE. Elsewhere, sequence diverge and length variation are substantial. Members of this family are mostly bacterial, largely absent from the Firmicutes and otherwise usually present. A few eukaryotic examples are found among the Apicomplexa, and a few archaeal sequences are found. Two functions implicated for this folate-binding protein are RNA modification (a function likely to be conserved) and replication initiation (a function likely to be highly variable). Many members of this family are, at the time of construction of this model, misnamed as the glycine cleavage system T protein.
tRNA-modifying protein YgfZ
tRNA-modifying protein YgfZ is a folate-dependent protein that participates in the assembly or repair of iron/sulphur clusters and is involved in the modification of some tRNAs
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on