Subtilisin
From Proteopedia
(Difference between revisions)
| Line 11: | Line 11: | ||
== Structural highlights == | == Structural highlights == | ||
The active site of Sub contains the <scene name='43/430882/Cv/12'>catalytic triad: Ser-His-Asp</scene>. The <scene name='43/430882/Cv/13'>peptide inhibitor has numerous interactions with Sub</scene> and the <scene name='43/430882/Cv/14'>scissile bond is flanked by Cys-Pro-Met-Val</scene><ref>PMID:1920411</ref>. | The active site of Sub contains the <scene name='43/430882/Cv/12'>catalytic triad: Ser-His-Asp</scene>. The <scene name='43/430882/Cv/13'>peptide inhibitor has numerous interactions with Sub</scene> and the <scene name='43/430882/Cv/14'>scissile bond is flanked by Cys-Pro-Met-Val</scene><ref>PMID:1920411</ref>. | ||
| + | |||
| + | == 3D Structures of Subtilisin == | ||
| + | [[Subtilisin 3D structures]] | ||
| + | |||
</StructureSection> | </StructureSection> | ||
| Line 22: | Line 26: | ||
**[[2z2x]] – TkSub - ''Thermococcus kodakarensis''<br /> | **[[2z2x]] – TkSub - ''Thermococcus kodakarensis''<br /> | ||
**[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br /> | **[[1sca]], [[1scb]], [[1sbc]], [[3unx]] – BsSub - ''Bacillus subtilis'' (Subtilisin Carlsberg)<br /> | ||
| + | **[[6pak]] - BsSub E (mutant)<br /> | ||
**[[1pxq]] – BsSub - NMR<br /> | **[[1pxq]] – BsSub - NMR<br /> | ||
**[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub - ''Bacillus amyloliquefaciens''<br /> | **[[1gns]], [[1sup]], [[1st2]], [[1s01]], [[1sbt]], [[2sbt]], [[2st1]] – BaSub - ''Bacillus amyloliquefaciens''<br /> | ||
| Line 43: | Line 48: | ||
* Mature subtilisin complexed with its propeptide | * Mature subtilisin complexed with its propeptide | ||
| - | **[[3cnq]] – BaSub<br /> | + | **[[3cnq]], [[5ox2]] – BaSub + prodomain<br /> |
| - | **[[1spb]] – BaSub (mutant)<br /> | + | **[[1spb]] – BaSub (mutant) + prodomain<br /> |
| - | **[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub<br /> | + | **[[3a3n]], [[3a3o]], [[3a3p]], [[2z56]], [[2z57]], [[2z58]], [[2z2y]], [[2z30]] – TkSub + prodomain<br /> |
| - | **[[3vv2]] – TkSub (mutant)<br /> | + | **[[3vv2]] – TkSub (mutant) + prodomain<br /> |
| - | **[[1scj]] – BsSub | + | **[[1scj]] – BsSub + prodomain<br /> |
* Subtilisin complexed with polypeptide inhibitor | * Subtilisin complexed with polypeptide inhibitor | ||
Revision as of 08:57, 10 February 2020
| |||||||||||
3D Structures of Subtilisin
Updated on 10-February-2020
References
- ↑ Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. J Biol Chem. 1968 May 10;243(9):2184-91. PMID:4967581
- ↑ Bell IM, Fisher ML, Wu ZP, Hilvert D. Kinetic studies on the peroxidase activity of selenosubtilisin. Biochemistry. 1993 Apr 13;32(14):3754-62. PMID:8385489
- ↑ Garcia-Mora P, Penas E, Frias J, Martinez-Villaluenga C. Savinase, the most suitable enzyme for releasing peptides from lentil (Lens culinaris var. Castellana) protein concentrates with multifunctional properties. J Agric Food Chem. 2014 May 7;62(18):4166-74. doi: 10.1021/jf500849u. Epub 2014, Apr 28. PMID:24738747 doi:http://dx.doi.org/10.1021/jf500849u
- ↑ Takeuchi Y, Satow Y, Nakamura KT, Mitsui Y. Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution. J Mol Biol. 1991 Sep 5;221(1):309-25. PMID:1920411
