TY - JOUR
T1 - High resolution crystal structure of ferricytochrome c' from Rhodobacter sphaeroides
AU - M.-Ramirez, Laura
AU - Axelrod, Herbert L.
AU - Herron, Steven R.
AU - Rupp, Bernhard
AU - Allen, James
AU - Kantardjieff, Katherine A.
N1 - Funding Information:
We thank the W.M. Keck Foundation and the California State University Program for Education and Research in Biotechnology (CSUPERB) for support of the Center for Molecular Structure. LMR was supported by a grant from the National Institutes of Health Minority Scientist Development Program (R25 GM56820). HLA and SRH were supported by California State University Fullerton. We thank Drs George Feher and Ed Abresch for access to bacterial growth facilities at UCSD; Drs Christopher Meyer and Brian Schick for helpful discussion, and Brad Van Mourik for computer support; Rebecca Baumbach, Cari Eldred, Mai Hua, Mei Liu, and Dorothy Rodriguez for their contributions to this project. LLNL is operated by the University of California for the US DOE under contract W-7405-ENG-48.
PY - 2003/6
Y1 - 2003/6
N2 - Cytochrome c' isolated from Rhodobacter sphaeroides strain R26 (RSCP) crystallizes as a dimer of two identical 14-kDa subunits, in trigonal space group P31, with cell parameters a, b = 48.10 Å, c = 115.80 Å. The crystal structure of RSCP has been solved by molecular replacement using cytochrome c' from Rhodobacter capsulatus (PDB ID: 1CPQ) as a search model. To ensure effective phase bias removal, the RSCP model was iteratively built into maps generated by a modified wARP procedure, Shake&wARP. The 1.8 Å model (PDB ID: 1GQA) has been refined to an R = 0.204 and freeR = 0.254. Each subunit consists of four antiparallel α-helices, with the pentacoordinate heme covalently bound to a C-X-Y-C-H motif near the C-terminus. F14, located on helix A, blocks direct access to what would be the sixth "distal" ligand binding site of the heme. The dimer subunits form a flattened "X" shape, intermediate between the Type 1 and Type 2 cytochromes c'. The presence of the aromatic F14 and a deep channel between helices B and C places RSCP into Group 1 cytochromes c'. Clear electron density has revealed that the amino acid sequences for the cytochrome c' from strains R26 and 2.4.1 are identical.
AB - Cytochrome c' isolated from Rhodobacter sphaeroides strain R26 (RSCP) crystallizes as a dimer of two identical 14-kDa subunits, in trigonal space group P31, with cell parameters a, b = 48.10 Å, c = 115.80 Å. The crystal structure of RSCP has been solved by molecular replacement using cytochrome c' from Rhodobacter capsulatus (PDB ID: 1CPQ) as a search model. To ensure effective phase bias removal, the RSCP model was iteratively built into maps generated by a modified wARP procedure, Shake&wARP. The 1.8 Å model (PDB ID: 1GQA) has been refined to an R = 0.204 and freeR = 0.254. Each subunit consists of four antiparallel α-helices, with the pentacoordinate heme covalently bound to a C-X-Y-C-H motif near the C-terminus. F14, located on helix A, blocks direct access to what would be the sixth "distal" ligand binding site of the heme. The dimer subunits form a flattened "X" shape, intermediate between the Type 1 and Type 2 cytochromes c'. The presence of the aromatic F14 and a deep channel between helices B and C places RSCP into Group 1 cytochromes c'. Clear electron density has revealed that the amino acid sequences for the cytochrome c' from strains R26 and 2.4.1 are identical.
KW - Cytochrome c'
KW - Four helix bundle
KW - Heme protein
KW - Rhodobacter sphaeroides
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U2 - 10.1023/A:1024286215637
DO - 10.1023/A:1024286215637
M3 - Article
AN - SCOPUS:1642455875
SN - 1074-1542
VL - 33
SP - 413
EP - 424
JO - Journal of Chemical Crystallography
JF - Journal of Chemical Crystallography
IS - 5-6
ER -