This entry represents the N-terminal domain of the decaheme cytochrome c component MtrC from the MtrCAB complex and its homologue MtrF, which is part of the MtrFDE complex. In Shewanella oneidensis, these proteins are at bacterial cell surface at the termini of trans-outer-membrane electron transfer conduits and allow the utilization of extracellular mineral forms of iron and manganese as respiratory electron acceptors [1-4]. MtrC/MtrF consist of four domains: domain I and III containing seven antiparallel beta-strands in an extended Greek key topology; domains II and IV each bind five tightly packed hemes covalently attached to the Cys residues of the five CXXCH motifs in each domain and form the central core, flanked by domains I and III [1-4]. This entry represents domain I (N-terminal) of MtrC/MtrF. Paper describing PDB structure 3pmq. [1]. 21606337. Structure of a bacterial cell surface decaheme electron conduit. Clarke TA, Edwards MJ, Gates AJ, Hall A, White GF, Bradley J, Reardon CL, Shi L, Beliaev AS, Marshall MJ, Wang Z, Watmough NJ, Fredrickson JK, Zachara JM, Butt JN, Richardson DJ;. Proc Natl Acad Sci U S A. 2011;108:9384-9389. Paper describing PDB structure 4lm8. [2]. 26126857. Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer. Edwards MJ, White GF, Norman M, Tome-Fernandez A, Ainsworth E, Shi L, Fredrickson JK, Zachara JM, Butt JN, Richardson DJ, Clarke TA;. Sci Rep. 2015;5:11677. Paper describing PDB structure 6qyc. [3]. 32289252. The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire. Edwards MJ, White GF, Butt JN, Richardson DJ,. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-10-16