BMC domain

BMC
carboxysome shell protein ccmk2
Identifiers
Symbol BMC
Pfam PF00936
InterPro IPR000249
PROSITE PDOC00876

Bacterial Microcompartment (BMC) domain is a protein domain found in a variety of shell proteins, including CsoS1A, CsoS1B and CsoS1C of Thiobacillus neapolitanus (Halothiobacillus neapolitanus) and their orthologs from other bacteria. These shell proteins form the polyhedral structure of organelle that play a metabolic role in bacteria. BMC domain consists of about 90 amino acid residues, characterized by β-α-β motif connected by a β-hairpin.

Majority of the shell proteins consist of a single BMC domain in each subunit, forming a hexameric structure that assemble to form the flat facets of the polyhedral shell.[1] To date, two shell proteins were found to consist a tandem BMC domains, of which forms a trimeric structure, giving a pseudo-hexameric appearance.[2][3]

References

  1. ^ Kerfeld, C. A.; Sawaya, M. R.; Tanaka, S.; Nguyen, C. V.; Phillips, M.; Beeby, M.; Yeates, T. O. (2005). "Protein Structures Forming the Shell of Primitive Bacterial Organelles". Science 309 (5736): 936–938. doi:10.1126/science.1113397. PMID 16081736.  edit
  2. ^ Heldt, D.; Frank, S.; Seyedarabi, A.; Ladikis, D.; Parsons, J. B.; Warren, M. J.; Pickersgill, R. W. (2009). "Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization inClostridium kluyveri". Biochemical Journal 423 (2): 199–207. doi:10.1042/BJ20090780. PMID 19635047.  edit
  3. ^ Pang, A.; Warren, M. J.; Pickersgill, R. W. (2011). "Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe–4S cluster-binding site". Acta Crystallographica Section D Biological Crystallography 67 (2): 91–96. doi:10.1107/S0907444910050201. PMID 21245529.  edit

This article incorporates text from the public domain Pfam and InterPro IPR000249