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[[Image:1wmd.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1wmd|  PDB=1wmd  |  SCENE=  }}  
{{STRUCTURE_1wmd|  PDB=1wmd  |  SCENE=  }}  


'''Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)'''
===Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K)===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15342641 15342641]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15342641 15342641]
Crystallization and preliminary X-ray diffraction studies of a novel alkaline serine protease (KP-43) from alkaliphilic Bacillus sp. strain KSM-KP43., Nonaka T, Fujihashi M, Kita A, Saeki K, Ito S, Miki K, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):717-8. Epub 2001, Apr 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11320315 11320315]
[[Category: Bacteria]]
[[Category: Bacteria]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alpha-beta hydrolase fold]]
[[Category: Alpha-beta hydrolase fold]]
[[Category: Jelly-roll beta-barrel]]
[[Category: Jelly-roll beta-barrel]]
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