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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Suga M,Lai TL,Sugiura M,Shen JR,Boussac Adoi
10.1016/j.febslet.2013.08.023subject
Has Abstractpub_date
2013-10-01 00:00:00pages
3267-72issue
19eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00637-6journal_volume
587pub_type
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