Cytochrome c3 from Desulfovibrio gigas: Crystal structure at 1.8 Å resolution and evidence for a specific calcium‐binding site
Cytochrome c3 from Desulfovibrio gigas: Crystal structure at 1.8 Å resolution and evidence for a specific calcium‐binding site
复制标题
来自 Desulfovibrio gigas 的细胞色素 c3:1.8 Å 分辨率的晶体结构和特定钙结合位点的证据
DOI:
10.1002/pro.5560050713
复制
发表时间:
1996
期刊:
影响因子:
8
通讯作者:
L. Sieker
中科院分区:
文献类型:
--
作者:
P. Matias;J. Morais;R. Coelho;M. A. Carrondo;K. Wilson;Z. Dauter;L. Sieker
Crystals of the tetraheme cytochrome c3 from sulfate‐reducing bacteria Desulfovibrio gigas (Dg) (MW 13 kDa, 111 residues, four heme groups) were obtained and X‐ray diffraction data collected to 1.8 Å resolution. The structure was solved by the method of molecular replacement and the resulting model refined to a conventional R‐factor of 14.9%. The three‐dimensional structure shows many similarities to other known crystal structures of tetraheme c3 cytochromes, but it also shows some remarkable differences. In particular, the location of the aromatic residues around the heme groups, which may play a fundamental role in the electron transfer processes of the molecule, are well conserved in the cases of hemes I, III, and IV. However, heme II has an aromatic environment that is completely different to that found in other related cytochromes c3. Another unusual feature is the presence of a Ca2+ ion coordinated by oxygen atoms supplied by the protein within a loop near the N‐terminus. It is speculated that this loop may be stabilized by the presence of this Ca2+ ion, may contribute to heme‐redox perturbation, and might even be involved in the specificity of recognition with its redox partner.
DOI:
10.1042/bj2940909
发表时间:
1993
期刊:
The Biochemical journal
影响因子:
--
作者:
Piçarra-Pereira,MA;Turner,DL;LeGall,J;Xavier,AV
通讯作者:
Xavier,AV
DOI:
10.1016/s0006-291x(05)81282-3
发表时间:
1991
影响因子:
3.1
作者:
Chen,L;Liu,MY;LeGall,J
通讯作者:
LeGall,J