caa a22 4500 445889527 CHVBK 20180317145611.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s11120-011-9624-6 doi (NATIONALLICENCE)springer-10.1007/s11120-011-9624-6 Comparative analysis of carboxysome shell proteins [Elektronische Daten] [James Kinney, Seth Axen, Cheryl Kerfeld] Carboxysomes are metabolic modules for CO2 fixation that are found in all cyanobacteria and some chemoautotrophic bacteria. They comprise a semi-permeable proteinaceous shell that encapsulates ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase. Structural studies are revealing the integral role of the shell protein paralogs to carboxysome form and function. The shell proteins are composed of two domain classes: those with the bacterial microcompartment (BMC; Pfam00936) domain, which oligomerize to form (pseudo)hexamers, and those with the CcmL/EutN (Pfam03319) domain which form pentamers in carboxysomes. These two shell protein types are proposed to be the basis for the carboxysome's icosahedral geometry. The shell proteins are also thought to allow the flux of metabolites across the shell through the presence of the small pore formed by their hexameric/pentameric symmetry axes. In this review, we describe bioinformatic and structural analyses that highlight the important primary, tertiary, and quaternary structural features of these conserved shell subunits. In the future, further understanding of these molecular building blocks may provide the basis for enhancing CO2 fixation in other organisms or creating novel biological nanostructures. The Author(s), 2011 Carboxysome nationallicence CO2 fixation nationallicence Bacterial microcompartment nationallicence Dark reactions nationallicence Cyanobacteria nationallicence Calvin cycle nationallicence Chemoautotroph nationallicence RuBisCO : Ribulose bisphosphate carboxylase/oxygenase nationallicence RuBP : Ribulose-1,5-bisphosphate nationallicence 3PGA : 3-Phosphoglycerate nationallicence CA : Carbonic anhydrase nationallicence HMM : Hidden Markov model nationallicence PDB : Protein Data Bank nationallicence BMC : Bacterial microcompartment nationallicence RMSD : Root mean square deviation nationallicence CCM : Carbon concentrating mechanism nationallicence ORF : Open reading frame nationallicence pdu : Propanediol utilization nationallicence eut : Ethanolamine utilization nationallicence Kinney James Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut Axen Seth Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut Kerfeld Cheryl Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut Photosynthesis Research Springer Netherlands 109/1-3(2011-09-01), 21-32 0166-8595 109:1-3<21 2011 109 11120 https://doi.org/10.1007/s11120-011-9624-6 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11120-011-9624-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kinney James Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut NATIONALLICENCE 700 1- Axen Seth Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut NATIONALLICENCE 700 1- Kerfeld Cheryl Department of Energy, Joint Genome Institute, 2800 Mitchell Drive, 94598, Walnut Creek, CA, USA aut NATIONALLICENCE 773 0- Photosynthesis Research Springer Netherlands 109/1-3(2011-09-01), 21-32 0166-8595 109:1-3<21 2011 109 11120 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer