1wmd

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spinqualitylabelsall models 1wmd, resolution 1.30Å 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 (1.30 angstrom, 100 K)

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

1WMD is a Single protein structure of sequence from Bacteria with CA, SO4, 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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