EMSL Scientific Grand Challenge: Membrane Biology
Membrane Biology GC Resources
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- What Are Cyanobacteria?
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Additional Information
Achievements: Structures
Cyanothece
Cyanothece 51142 genome
Rfr23
At left is a cartoon representation of the structure of Rfr23 (2O6W) colored spectrally (roygbiv) from the C-terminus. The structure is dominated by an Rfr-fold composed of nearly six complete coils, C1 to C6. At one corner of the Rfr-fold, between coils C1 and C2, is a 24-residue loop for which little electron density was observed. In the C-terminal coil, C6, there is a small perturbation to the Rfr-fold labeled a “single-residue loop”. Not shown is a “disulfide bracket” in one corner of the first coil (C39-C42).
Buchko GW, H Robinson, S Ni, HB Pakrasi, and MA Kennedy. 2006. "Cloning, expression, crystallization, and preliminary crystallographic analysis of a pentapeptide repeat protein (Rfr23) from bacterium Cyanothece 51142." Acta Cryst. (2006) F62:1251-1254. Abstract
Rfr32
Buchko GW, S Ni, H Robinson, EA Welsh, HB Pakrasi, and MA Kennedy. 2006. "Characterization of two potentially universal turn motifs that shape the repeated five-residues fold - Crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142." Protein Sci (2006) 15:2579-2595. Abstract
Synechocystis
Two ABC transporter solute-binding proteins, including one crucial for cyanobacterial carbon sequestration:
NrtA
Koropatkin NM, Pakrasi HB, Smith TJ. "Atomic structure of a nitrate-binding protein crucial for photosynthetic productivity." Proceedings of the National Academy of Sciences of the United States of America 103 (26): 9820-9825 Jun 27 2006. Abstract
CmpA
Koropatkin, NM, DW Koppenaal, HB Pakrasi & TJ Smith. 2007. "The Structure of a Cyanobacterial Bicarbonate Transport Protein, CmpA." J. Biol. Chem., 282(4):2607-2614. Abstract
