2I8F

Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551

Summary for 2I8F

• Entry DOI: 10.2210/pdb2i8f/pdb
• Related: 1CCH
• NMR Information: BMRB: 7296
• Descriptor: Cytochrome c-551, HEME C (2 entities in total)
• Functional Keywords: helix-turn-helix, cytochrome, electron transport
• Biological source: Pseudomonas stutzeri ZoBell
• Cellular location: Periplasm: P00101
• Total number of polymer chains: 1
• Total formula weight: 9124.29

Authors

Liang, Q.,Timkovich, R. (deposition date: 2006-09-01, release date: 2007-06-05, Last modification date: 2024-11-20)

Primary citation

Liang, Q.,Miller, G.T.,Beeghley, C.A.,Graf, C.B.,Timkovich, R.
Solution Conformation of the His-47 to Ala-47 Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551.
Biophys.J., 93:1700-1706, 2007

PubMed Abstract: In the cytochrome c-551 family, the heme 17-propionate caboxylate group is always hydrogen bonded to an invariant Trp-56 and conserved residues (His and Arg mainly, Lys occasionally) at position 47. The mutation of His-47 to Ala-47 for Pseudomas stutzeri ZoBell cytochrome c-551 removes this otherwise invariant hydrogen bond. The solution structure of ferrous H47A has been solved based on NMR-derived constraints. Results indicate that the mutant has very similar main chain folding compared to wild-type. However, less efficient packing of residues in the mutant surrounding the heme propionates leads to more solvent exposure for both propionate groups, which may account for decreased stability of the mutant. The mutant has a reduction potential different from wild-type, and furthermore, the pH dependence of this potential is not the same as for wild-type. The structure of the mutant suggests that these changes are related to the loss of the residue-47 propionate hydrogen bond and the loss of charge on the side chain of residue 47.

PubMed: 17496029
DOI: 10.1529/biophysj.106.102772

Experimental method

SOLUTION NMR