1MZ4

Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus

Summary for 1MZ4

• Entry DOI: 10.2210/pdb1mz4/pdb
• Related: 1e29 1f1c
• Descriptor: cytochrome c550, PHOSPHATE ION, BICARBONATE ION, ... (6 entities in total)
• Functional Keywords: psii associated cytochrome, electron transport
• Biological source: Thermosynechococcus elongatus
• Cellular location: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side: P0A386
• Total number of polymer chains: 1
• Total formula weight: 16763.10

Authors

Kerfeld, C.A.,Sawaya, M.R.,Bottin, H.,Tran, K.T.,Sugiura, M.,Kirilovsky, D.,Krogmann, D.,Yeates, T.O.,Boussac, A. (deposition date: 2002-10-05, release date: 2003-09-23, Last modification date: 2024-11-06)

Primary citation

Kerfeld, C.A.,Sawaya, M.R.,Bottin, H.,Tran, K.T.,Sugiura, M.,Cascio, D.,Desbois, A.,Yeates, T.O.,Kirilovsky, D.,Boussac, A.
Structural and EPR characterization of the soluble form of cytochrome c-550 and of the psbV2 gene product from the cyanobacterium Thermosynechococcus elongatus.
Plant Cell.Physiol., 44:697-706, 2003

PubMed Abstract: First, the crystal structure of cytochrome c-550 (the psbV1 gene product) from the thermophilic cyanobacterium Thermosynechococcus elongatus has been determined to a resolution of 1.8 A. A comparison of the T. elongatus cytochrome c-550 structure to its counterparts from mesophilic organisms, Synechocystis 6803 and Arthrospira maxima, suggests that increased numbers of hydrogen bonds may play a role in the structural basis of thermostability. The cytochrome c-550 in T. elongatus also differs from that in Synechocystis 6803 and Arthrospira maxima in its lack of dimerization and the presence of a trigonal planar molecule, possibly bicarbonate, tightly bound to the heme propionate oxygen atoms. Cytochromes c-550 from T. elongatus, Synechocystis 6803 and Arthrospira maxima exhibit different EPR spectra. A correlation has been done between the heme-axial ligands geometries and the rhombicity calculated from the EPR spectra. This correlation indicates that binding of cytochrome c-550 to Photosystem II is accompanied by structural changes in the heme vicinity. Second, the psbV2 gene product has been found and purified. The UV-visible, EPR and Raman spectra are reported. From the spectroscopic data and from a theoretical structural model based on the cytochrome c-550 structure it is proposed that the 6th ligand of the heme-iron is the Tyr86.

PubMed: 12881497
DOI: 10.1093/pcp/pcg084

Experimental method

X-RAY DIFFRACTION (1.8 Å)