5E3X

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

Summary for 5E3X

• Entry DOI: 10.2210/pdb5e3x/pdb
• Descriptor: Thermostable carboxypeptidase 1, COBALT (II) ION (3 entities in total)
• Functional Keywords: carboxypeptidase, fervidobacterium, fiscp, hydrolase
• Biological source: Fervidobacterium islandicum
• Total number of polymer chains: 1
• Total formula weight: 57375.08

Authors

Dhanasingh, I.,Lee, Y.-J.,Lee, D.W.,Lee, S.H. (deposition date: 2015-10-05, release date: 2016-02-10, Last modification date: 2023-11-08)

Primary citation

Lee, Y.-J.,Dhanasingh, I.,Ahn, J.-S.,Jin, H.-S.,Choi, J.M.,Lee, S.H.,Lee, D.-W.
Biochemical and structural characterization of a keratin-degrading M32 carboxypeptidase from Fervidobacterium islandicum AW-1
Biochem.Biophys.Res.Commun., 468:927-933, 2015

PubMed Abstract: 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 °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 Å resolution showed high levels of structural similarities (root-mean-square deviations of <1.7 Å) 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.

PubMed: 26603937
DOI: 10.1016/j.bbrc.2015.11.058

Experimental method

X-RAY DIFFRACTION (2.197 Å)