Monday, October 29, 2012

Undecahaem cytochrome from Shewanella

The first crystal structures of the 11-haem cytochrome from Shewanella sp. strain HRCR-6 have been solved [1], both ligand-free [2] and in complex with iron chelates Fe(III)-citrate [3] and Fe(III)-nitrilotriacetate [4]. The authors propose that

the region around heme 7 could be a rudimentary active site for association of soluble organic redox partners, which would be consistent with the UndA functioning as an enzyme with broad, but differential, specificity to a variety of substrates, in contrast to a nonspecific cathode on the cell surface <such as decaheme cytochrome MtrF>.

  1. Edwards, M.J., Hall, A., Shi, L., Fredrickson, J.K., Zachara, J.M., Butt, J.N., Richardson, D.J. and Clarke, T.A. (2012) The crystal structure of the extracellular 11-heme cytochrome UndA reveals a conserved 10-heme motif and defined binding site for soluble iron chelates. Structure 20, 1275—1284.
  2. PDB:3UCP
  3. PDB:3UFH
  4. PDB:3UFK

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