4pf1

Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon

spinqualitylabelsall models 4pf1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pf1 is a 4 chain structure with sequence from Thaumarchaeota archaeon e09. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, PGE Gene: MCGE09_00221 (Thaumarchaeota archaeon E09) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Marine sediments host a large population of diverse, heterotrophic, uncultured microorganisms with unknown physiologies that control carbon flow through organic matter decomposition. Recently, single-cell genomics uncovered new key players in these processes, such as the miscellaneous crenarchaeotal group. These widespread archaea encode putative intra- and extracellular proteases for the degradation of detrital proteins present in sediments. Here, we show that one of these enzymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrophobic residues at the N terminus of the hydrolyzed peptide. The ability to perform detailed characterizations of enzymes from native subsurface microorganisms, without requiring that those organisms first be grown in pure culture, holds great promise for understanding key carbon transformations in the environment as well as identifying new enzymes for biomedical and biotechnological applications. New aminopeptidase from "microbial dark matter" archaeon.,Michalska K, Steen AD, Chhor G, Endres M, Webber AT, Bird J, Lloyd KG, Joachimiak A FASEB J. 2015 Sep;29(9):4071-9. doi: 10.1096/fj.15-272906. Epub 2015 Jun 10. PMID:26062601 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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