1yja

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yja.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1yja.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yja| PDB=1yja | SCENE= }}
{{STRUCTURE_1yja| PDB=1yja | SCENE= }}
-
'''SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 20% DIMETHYLFORMAMIDE'''
+
===SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 20% DIMETHYLFORMAMIDE===
-
==Overview==
+
<!--
-
The serine protease subtilisin BPN' is a useful catalyst for peptide synthesis when dissolved in high concentrations of a water-miscible organic co-solvent such as N,N-dimethylformamide (DMF). However, in 50% DMF, the k(cat) for amide hydrolysis is two orders of magnitude lower than in aqueous solution. Surprisingly, the k(cat) for ester hydrolysis is unchanged in 50% DMF. To explain this alteration in activity, the structure of subtilisin 8397+1 was determined in 20, 35, and 50% (v/v) DMF to 1.8 A resolution. In 50% DMF, the imidazole ring of His64, the central residue of the catalytic triad, has rotated approximately 180 degrees around the Cbeta-Cgamma bond. Two new water molecules in the active site stabilize the rotated conformation. This rotation places His64 in an unfavorable geometry to interact with the other members of the catalytic triad, Ser221 and Asp32. NMR experiments confirm that the characteristic resonance due to the low barrier hydrogen bond between the His64 and Asp32 is absent in 50% DMF. These experiments provide a clear structural basis for the change in activity of serine proteases in organic co-solvents.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10048334}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10048334 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10048334}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Sporulation]]
[[Category: Sporulation]]
[[Category: Zymogen]]
[[Category: Zymogen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:23:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:40:54 2008''

Revision as of 08:40, 29 July 2008

Image:1yja.png

Template:STRUCTURE 1yja

SUBTILISIN BPN' 8397+1 (E.C. 3.4.21.14) (MUTANT WITH MET 50 REPLACED BY PHE, ASN 76 REPLACED BY ASP, GLY 169 REPLACED BY ALA, GLN 206 REPLACED BY CYS, ASN 218 REPLACED BY SER AND LYS 256 REPLACED BY TYR) (M50F, N76D, G169A, Q206C, N218S, AND K256Y) IN 20% DIMETHYLFORMAMIDE

Template:ABSTRACT PUBMED 10048334

About this Structure

1YJA is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Breaking the low barrier hydrogen bond in a serine protease., Kidd RD, Sears P, Huang DH, Witte K, Wong CH, Farber GK, Protein Sci. 1999 Feb;8(2):410-7. PMID:10048334

Page seeded by OCA on Tue Jul 29 11:40:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yja"
Personal tools