|
|
| Line 1: |
Line 1: |
| [[Image:1wmf.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1wmf.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1wmf| PDB=1wmf | SCENE= }} | | {{STRUCTURE_1wmf| PDB=1wmf | SCENE= }} |
|
| |
|
| '''Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom)'''
| | ===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. | | The line below this paragraph, {{ABSTRACT_PUBMED_15342641}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15342641 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15342641}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| [[Category: Alpha-beta hydrolase fold]] | | [[Category: Alpha-beta hydrolase fold]] |
| [[Category: Jelly-roll beta-barrel]] | | [[Category: Jelly-roll beta-barrel]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:52:27 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:21:01 2008'' |
