This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1e2z
From Proteopedia
|
Q158L MUTANT OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII
Overview
The structure of cytochrome f includes an internal chain of five water, molecules and six hydrogen-bonding side chains, which are conserved, throughout the phylogenetic range of photosynthetic organisms from higher, plants, algae, and cyanobacteria. The in vivo electron transfer capability, of Chlamydomonas reinhardtii cytochrome f was impaired in site-directed, mutants of the conserved Asn and Gln residues that form hydrogen bonds, with water molecules of the internal chain [Ponamarev, M. V., and Cramer, W. A. (1998) Biochemistry 37, 17199-17208]. The 251-residue extrinsic, functional domain of C. reinhardtii cytochrome f was expressed in, Escherichia coli without the 35 C-terminal residues of the intact, cytochrome that contain the membrane anchor. Crystal structures were, determined ... [(full description)]
About this Structure
1E2Z is a [Single protein] structure of sequence from [Chlamydomonas reinhardtii] with HEC as [ligand]. Structure known Active Sites: AC2 and AC3. Full crystallographic information is available from [OCA].
Reference
Interruption of the internal water chain of cytochrome f impairs photosynthetic function., Sainz G, Carrell CJ, Ponamarev MV, Soriano GM, Cramer WA, Smith JL, Biochemistry. 2000 Aug 8;39(31):9164-73. PMID:10924110
Page seeded by OCA on Tue Oct 30 12:36:02 2007
