A carboxypeptidase is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of carboxypeptidases that have diverse functions ranging from catabolism to protein maturation.(read more DOI: 10.1038/nature06956 and Wikipedia)
This crystal structure belongs to the Neuraminidase such a surprising vegetable.
Neuraminidase is a key protein of influenza viruses and in this structure one inhibitor is also present bound to it. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. The study of neuraminidases and how they evolve, and the research of novel inhibitors are key for having antiviral drugs in the future (read more DOI: 10.1038/nature06956 and Wikipedia)
Potato (Solanum tuberosum) multicystatin an inhibitor of protease of the family Cys protease and found in the subphellogen layer of potato tubers. In contrast with cystatins from other plant and animal sources, this protein has a high molecular mass of 85 kDa/monomer, compared to 8 or 25 kDa. It can also bind and inhibit several Cys proteases (e.g., papain) simultaneously, and the term multicystatin thus refers to its multiple inhibitory domains (read more DOI: 10.1105/tpc.108.064717 and doi: 10.1105/tpc.108.064717)
Lipocalins are extracellular proteins (17-25 kDa) that bind and transport small lipophilic molecules. Trichosurin, a protein from the milk whey of the common brushtail possum (read more DOI: 10.1042/BJ20070567 or PMC2049081/)
CcmK4 is a protein forming the shell of protein-only bacterial organelles. these organelles are called microcompartments and are self-assembling (how amazing?) (read more DOI: 10.1021/sb500226j and Wikipedia)