| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 263, Issue 16, 7895-7906, Jun, 1988
R Bott, M Ultsch, A Kossiakoff, T Graycar, B Katz and S Power
The three-dimensional structure of the subtilisin from Bacillus
amyloliquefaciens (BAS) has been refined to 1.8 A using the amino acid
sequence deduced from the DNA coding sequence. The structure is essentially
the same as the previously reported structures of subtilisin BPN' (Wright,
C.S., Alden, R.A., and Kraut, J. (1969) Nature 221, 235-242) and Novo
(Drenth, J., Hol, W. G. J., Jansonius, J. N., and Koekoek, R. (1972) Eur.
J. Biochem. 26, 177-181) determined in different crystal forms, at 2.5 and
2.8 A resolution, respectively. The largest differences in the three
crystallographic models are seen in regions where the amino acid sequence
used in the fit to the electron density maps of BPN' and Novo differs from
the gene sequence of BAS (Wells, J. A., Ferrari, E., Henner, D. J., Estell,
D. A., and Chen, E. Y. (1983) Nucleic Acids Res. 11, 7911-7925). The
refined BAS model shows new features of cation binding, hydrogen bonding,
and internal solvent structure. The refined BAS model has served as a basis
for the analysis of stereochemical factors involved in the peroxide
inactivation of the enzyme. Methionine 222, which is adjacent to the
catalytic Ser221, is quantitatively oxidized to the sulfoxide by hydrogen
peroxide as had been previously shown for the related Bacillus
licheniformis enzyme (Stauffer, C. E., and Etson, D. (1969) J. Biol. Chem.
244, 5333-5338). In addition to this site of modification, we observe
partial to full oxidation of two of the four remaining methionines. The
oxidation of the methionines does not correlate well with their solvent
accessibility calculated from the x-ray structure coordinates; in addition,
only one of the two possible stereoisomers of methionine sulfoxide is
formed. We also detect hydrogen peroxide- induced modification of the
hydroxyl groups of two tyrosines. Modeling suggests that most of the
observed effect of oxidation on the enzyme's catalytic efficiency can be
attributed to unfavorable interactions at the oxyanion binding site between
the sulfoxide group at 222 and the carbonyl oxygen of the scissile peptide
bond of the bound substrate.
The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 A and an analysis of the structural consequences of peroxide inactivation
Department of Biomolecular Chemistry, Genentech, Inc., South San Francisco, California 94080.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  B. Shao, A. Belaaouaj, C. L. M. J. Verlinde, X. Fu, and J. W. Heinecke Methionine Sulfoxide and Proteolytic Cleavage Contribute to the Inactivation of Cathepsin G by Hypochlorous Acid: AN OXIDATIVE MECHANISM FOR REGULATION OF SERINE PROTEINASES BY MYELOPEROXIDASE J. Biol. Chem., August 12, 2005; 280(32): 29311 - 29321. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Nonaka, M. Fujihashi, A. Kita, K. Saeki, S. Ito, K. Horikoshi, and K. Miki The Crystal Structure of an Oxidatively Stable Subtilisin-like Alkaline Serine Protease, KP-43, with a C-terminal {beta}-Barrel Domain J. Biol. Chem., November 5, 2004; 279(45): 47344 - 47351. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. M. Day, C. J. Thalhauser, J. L. Sudmeier, M. P. Vincent, E. V. Torchilin, D. G. Sanford, C. W. Bachovchin, and W. W. Bachovchin Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR Protein Sci., April 1, 2003; 12(4): 794 - 810. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Kannan, Y. Koga, Y. Inoue, M. Haruki, M. Takagi, T. Imanaka, M. Morikawa, and S. Kanaya Active Subtilisin-Like Protease from a Hyperthermophilic Archaeon in a Form with a Putative Prosequence Appl. Envir. Microbiol., June 1, 2001; 67(6): 2445 - 2452. [Abstract] [Full Text]
|
|
|
|
 |
|
 Y. H. Kim, A. H. Berry, D. S. Spencer, and W. E. Stites Comparing the effect on protein stability of methionine oxidation versus mutagenesis: steps toward engineering oxidative resistance in proteins Protein Eng. Des. Sel., May 1, 2001; 14(5): 343 - 347. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Atwell and J. A. Wells Selection for improved subtiligases by phage display PNAS, August 17, 1999; 96(17): 9497 - 9502. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Hu, K. Haghjoo, and F. Jordan Further Evidence for the Structure of the Subtilisin Propeptide and for Its Interactions with Mature Subtilisin J. Biol. Chem., February 16, 1996; 271(7): 3375 - 3384. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Cunningham and J. Wells High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis Science, June 2, 1989; 244(4908): 1081 - 1085. [Abstract] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
