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.
RuBisCO accumulation factor 1
This is the C-terminal domain, also known as the beta domain, of Rubsico Assembly Chaperone protein (Raf1). Raf1 is necessary for rubisco to catalyze the rate-limiting step of carbon fixation through carboxylating the five-carbon sugar substrate ribulose-1,5-bisphosphate. The beta domains primary function is dimerization, which is critical for Raf1 to achieve the necessary avidity for complex formation with RbcL (the large complex sub-unbit of Rubsico) assembly intermediates. The beta domain is also involved, to a small extent, in binding to RbcL with use of the lustiness near the beta domain's conserved top surface [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)
Rubisco accumulation factor 1 helix turn helix domain
This is helix turn helix domain found in alpha helical region of Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)
This is the N-terminal alpha helical domain found in Rubisco accumulation factor1 (Raf1). Raf1 from Arabidopsis thaliana consists of an N-terminal alpha-domain, a flexible linker segment and a C-terminal beta-sheet domain that mediates dimerization. The alpha-domains mediate the majority of functionally important contacts with RbcL (Rubisco large subunits) by bracketing each RbcL dimer at the top and bottom. The alpha-domain alone is essentially inactive [1]. [1]. 26237510. Structure and mechanism of the Rubisco-assembly chaperone Raf1. Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M;. Nat Struct Mol Biol. 2015;22:720-728. (from Pfam)
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on