1e2v
From Proteopedia
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Revision as of 12:59, 30 October 2007
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N153Q 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
1E2V is a [Single protein] structure of sequence from [Chlamydomonas reinhardtii] with ACT and HEC as [ligands]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. 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
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