4LJI

Crystal structure at 1.5 angstrom resolution of the PsbV2 cytochrome from the cyanobacterium thermosynechococcus elongatus

Summary for 4LJI

• Entry DOI: 10.2210/pdb4lji/pdb
• Descriptor: Cytochrome c-550-like protein, HEME C, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: cytochrome c, electron transport
• Biological source: Thermosynechococcus elongatus
• Total number of polymer chains: 2
• Total formula weight: 31978.77

Authors

Suga, M.,Lai, T.-L.,Sugiura, M.,Shen, J.-R.,Boussac, A. (deposition date: 2013-07-04, release date: 2013-08-28, Last modification date: 2023-11-08)

Primary citation

Suga, M.,Lai, T.-L.,Sugiura, M.,Shen, J.-R.,Boussac, A.
Crystal structure at 1.5 angstrom resolution of the PsbV2 cytochrome from the cyanobacterium Thermosynechococcus elongatus
Febs Lett., 587:3267-3272, 2013

PubMed Abstract: PsbV2 is a c-type cytochrome present in a very low abundance in the thermophilic cyanobacterium Thermosynechococcus elongatus. We purified this cytochrome and solved its crystal structure at a resolution of 1.5Å. The protein existed as a dimer in the crystal, and has an overall structure similar to other c-type cytochromes like Cytc6 and Cytc550, for example. However, the 5th and 6th heme iron axial ligands were found to be His51 and Cys101, respectively, in contrast to the more common bis-His or His/Met ligands found in most cytochromes. Although a few other c-type cytochromes were suggested to have this axial coordination, this is the first crystal structure reported for a c-type heme with this unusual His/Cys axial coordination. Previous spectroscopic characterizations of PsbV2 are discussed in relation to its structural properties.

PubMed: 23994160
DOI: 10.1016/j.febslet.2013.08.023

Experimental method

X-RAY DIFFRACTION (1.508 Å)