1wmf
From Proteopedia
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|PDB= 1wmf |SIZE=350|CAPTION= <scene name='initialview01'>1wmf</scene>, resolution 1.73Å | |PDB= 1wmf |SIZE=350|CAPTION= <scene name='initialview01'>1wmf</scene>, resolution 1.73Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SME:METHIONINE+SULFOXIDE'>SME</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1wmd|1WMD]], [[1wme|1WME]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmf OCA], [http://www.ebi.ac.uk/pdbsum/1wmf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wmf RCSB]</span> | ||
}} | }} | ||
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[[Category: Nonaka, T.]] | [[Category: Nonaka, T.]] | ||
[[Category: Saeki, K.]] | [[Category: Saeki, K.]] | ||
- | [[Category: CA]] | ||
- | [[Category: DIO]] | ||
- | [[Category: GOL]] | ||
[[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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:38:16 2008'' |
Revision as of 21:38, 30 March 2008
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, resolution 1.73Å | |||||||
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Ligands: | , , , | ||||||
Related: | 1WMD, 1WME
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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