5e3x

Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1Crystal structure of thermostable Carboxypeptidase (FisCP) from Fervidobacterium Islandicum AW-1

Structural highlights 5e3x is a 1 chain structure with sequence from Fervidobacterium islandicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.197Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A140UHP3_FERIS Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.[PIRNR:PIRNR006615] Publication Abstract from PubMed Comparative genomics of the keratin-degrading extremophilic eubacterium Fervidobacterium islandicum AW-1 and the closely related Fervidobacterium nodosum with no keratinolytic activity suggested that the FIAW1_1600 gene encoding a carboxypeptidase (CP) plays an important role in keratin degradation. The presumptive 489 amino acid sequence of the gene showed a conserved HEXXH motif with low levels of sequence identity (<38%) to reported thermostable M32 CPs. To identify its functional role, the FIAW1_1600 gene was overexpressed in Escherichia coli, and the recombinant enzyme was purified and characterized in detail. F. islandicum AW-1 CP (FisCP) formed a homodimer with a molecular mass of 107 kDa, and its apoenzyme exhibited maximal activity at 80 degrees C and pH 7.0 in the presence of Co(2+). This metalloenzyme mainly cleaved the C-termini of peptides with a basic amino acid sequence. The crystal structure of FisCP at 2.2 A resolution showed high levels of structural similarities (root-mean-square deviations of <1.7 A) to those of other M32 CP homologs. Remarkably, the enzyme significantly enhanced the degradation of native chicken feathers. This study suggests that FisCP, a keratinolytic member of the thermostable M32 CP family, plays an important role in keratin degradation for cellular metabolism in F. islandicum AW-1. Biochemical and structural characterization of a keratin-degrading M32 carboxypeptidase from Fervidobacterium islandicum AW-1.,Lee YJ, Dhanasingh I, Ahn JS, Jin HS, Choi JM, Lee SH, Lee DW Biochem Biophys Res Commun. 2015 Dec 25;468(4):927-33. doi:, 10.1016/j.bbrc.2015.11.058. Epub 2015 Nov 19. PMID:26603937 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carboxypeptidase 3D structures

spinqualitylabelsall models 5e3x, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image