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1.S.2.  The Bacterial Microcompartment Shell/Pore-forming Protein-2 (BMC-SP2) Family 

In contrast to the BMC-SP1 family which consists primarily of small proteins of about 100 aas, the BMC-SP2 family consists of proteins of somewhat greater than 200 aas and are only distantly homologous to the BMC-SP1 proteins. These two families probably comprise a superfamily.  However, they contribute to shell formation, sometimes in the same BMC shell as a BMC-SP1 protein as in the ethanolamine utilizing (Eut) BMC of E. coli, and both types of shell proteins form pores (Takenoya et al. 2010).  In contrast to EutL (BMC-SP1), the pore of EutM (BMC-SP2) appears to be positively charged, indicating specificity for different solutes.  Moreover, only the pore of EutL can be triggered to open by exposure to zinc ions (Takenoya et al. 2010).

This family belongs to the: BMC Shell Protein Superfamily.

References associated with 1.S.2 family:

Crowley, C.S., M.R. Sawaya, T.A. Bobik, and T.O. Yeates. (2008). Structure of the PduU shell protein from the Pdu microcompartment of Salmonella. Structure 16: 1324-1332. 18786396
Heldt, D., S. Frank, A. Seyedarabi, D. Ladikis, J.B. Parsons, M.J. Warren, and R.W. Pickersgill. (2009). Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri. Biochem. J. 423: 199-207. 19635047
Sagermann, M., A. Ohtaki, and K. Nikolakakis. (2009). Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc. Natl. Acad. Sci. USA 106: 8883-8887. 19451619
Takenoya, M., K. Nikolakakis, and M. Sagermann. (2010). Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli. J. Bacteriol. 192: 6056-6063. 20851901
Thompson, M.C., D. Cascio, D.J. Leibly, and T.O. Yeates. (2015). An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein. Protein. Sci. 24: 956-975. 25752492