4PF1
Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon
Summary for 4PF1
| Entry DOI | 10.2210/pdb4pf1/pdb |
| Descriptor | Peptidase S15/CocE/NonD, TRIETHYLENE GLYCOL, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | serine peptidase, single cell genomics, alpha/beta hydrolase fold, structural genomics, psi-biology, midwest center for structural genomics, mcsg, hydrolase |
| Biological source | Thaumarchaeota archaeon SCGC AB-539-E09 |
| Total number of polymer chains | 4 |
| Total formula weight | 287087.29 |
| Authors | Michalska, K.,Chhor, G.,Fayman, K.,Endres, M.,Jedrzejczak, R.,Babnigg, G.,Steen, A.,Lloyd, K.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2014-04-25, release date: 2014-06-11, Last modification date: 2023-09-27) |
| Primary citation | Michalska, K.,Steen, A.D.,Chhor, G.,Endres, M.,Webber, A.T.,Bird, J.,Lloyd, K.G.,Joachimiak, A. New aminopeptidase from "microbial dark matter" archaeon. FASEB J., 29:4071-4079, 2015 Cited by PubMed Abstract: 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. PubMed: 26062601DOI: 10.1096/fj.15-272906 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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