2BC5
Crystal structure of E. coli cytochrome b562 with engineered c-type heme linkages
Summary for 2BC5
| Entry DOI | 10.2210/pdb2bc5/pdb |
| Related | 256B |
| Descriptor | Soluble cytochrome b562, SULFATE ION, HEME C, ... (4 entities in total) |
| Functional Keywords | four-helix bundle, k59w, r98c and y101c mutations, electron transport |
| Biological source | Escherichia coli |
| Cellular location | Periplasm: P0ABE7 |
| Total number of polymer chains | 4 |
| Total formula weight | 50307.34 |
| Authors | Faraone-Mennella, J.,Tezcan, F.A.,Gray, H.B.,Winkler, J.R. (deposition date: 2005-10-18, release date: 2006-09-26, Last modification date: 2024-11-06) |
| Primary citation | Faraone-Mennella, J.,Tezcan, F.A.,Gray, H.B.,Winkler, J.R. Stability and Folding Kinetics of Structurally Characterized Cytochrome c-b(562). Biochemistry, 45:10504-10511, 2006 Cited by PubMed Abstract: The four-helix-bundle protein fold can be constructed from a wide variety of primary amino acid sequences. Proteins with this structure are excellent candidates for investigations of the relationship between folding mechanism and topology. The folding of cytochrome b(562), a four-helix-bundle heme protein, is hampered by heme dissociation. To overcome this complication, we have engineered a variant of cytochrome b(562) (cyt c-b(562)) featuring a c-type linkage between the heme and the polypeptide chain. The replacement of the native cyt b(562) leader sequence in this protein with that of a c-type cytochrome (cyt c(556)) led to high yields of fully matured and correctly folded cyt c-b(562). We have determined the X-ray crystal structure of cyt c-b(562) at 2.25 A and characterized its physical, chemical, and folding properties. These measurements reveal that the c-type linkage does not perturb the protein fold or reduction potential of the heme group. The covalent attachment of the porphyrin to the polypeptide does, however, produce a substantial change in protein stability and folding kinetics. PubMed: 16939202DOI: 10.1021/bi060242x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
Download full validation report
