1wmf

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spinqualitylabelsall models 1wmf, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom)

Overview

The crystal structure of an oxidatively stable subtilisin-like alkaline, serine protease, KP-43 from Bacillus sp. KSM-KP43, with a C-terminal, extension domain, was determined by the multiple isomorphous replacements, method with anomalous scattering. The native form was refined to a, crystallographic R factor of 0.134 (Rfree of 0.169) at 1.30-A resolution., KP-43 consists of two domains, a subtilisin-like alpha/beta domain and a, C-terminal jelly roll beta-barrel domain. The topological architecture of, the molecule is similar to that of kexin and furin, which belong to the, subtilisin-like proprotein convertases, whereas the amino acid sequence, and the binding orientation of the C-terminal beta-barrel domain both, differ in each case. Since the C-terminal domains of subtilisin-like, proprotein convertases are essential for folding themselves, the domain of, KP-43 is also thought to play such a role. KP-43 is known to be an, oxidation-resistant protease among the general subtilisin-like proteases., To investigate how KP-43 resists oxidizing reagents, the structure of, oxidized KP-43 was also determined and refined to a crystallographic R, factor of 0.142 (Rfree of 0.212) at 1.73-A resolution. The structure, analysis revealed that Met-256, adjacent to catalytic Ser-255, was, oxidized similarly to an equivalent residue in subtilisin BPN'. Although, KP-43, as well as proteinase K and subtilisin Carlsberg, lose their, hydrolyzing activity against synthetic peptides after oxidation treatment, all of them retain 70-80% activity against proteinaceous substrates. These, results, as well as the beta-casein digestion pattern analysis, have, indicated that the oxidation of the methionine adjacent to the catalytic, serine is not a dominant modification but might alter the substrate, specificities.

About this Structure

1WMF is a Single protein structure of sequence from Bacteria with CA, DIO and GOL as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal beta-barrel domain., Nonaka T, Fujihashi M, Kita A, Saeki K, Ito S, Horikoshi K, Miki K, J Biol Chem. 2004 Nov 5;279(45):47344-51. Epub 2004 Sep 1. PMID:15342641

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