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The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 Å resolution

Crennell, Susan; Hreggvidsson, Gudmundur and Nordberg Karlsson, Eva LU (2002) In Journal of Molecular Biology 320(4). p.883-897
Abstract
Cellulose is one of the most abundant polysaccharides in nature and microorganisms have developed a comprehensive system for enzymatic breakdown of this ubiquitous carbon source, a subject of much interest in the biotechnology industry. Rhodothermus marinus produces a hyperthermostable cellulase, with a temperature optimum of more than 90 °C, the structure of which is presented here to 1.8 Å resolution. The enzyme has been classified into glycoside hydrolase family 12; this is the first structure of a thermophilic member of this family to have been solved. The β-jelly roll fold observed has identical topology to those of the two mesophilic members of the family whose structures have been elucidated previously. A Hepes buffer molecule bound... (More)
Cellulose is one of the most abundant polysaccharides in nature and microorganisms have developed a comprehensive system for enzymatic breakdown of this ubiquitous carbon source, a subject of much interest in the biotechnology industry. Rhodothermus marinus produces a hyperthermostable cellulase, with a temperature optimum of more than 90 °C, the structure of which is presented here to 1.8 Å resolution. The enzyme has been classified into glycoside hydrolase family 12; this is the first structure of a thermophilic member of this family to have been solved. The β-jelly roll fold observed has identical topology to those of the two mesophilic members of the family whose structures have been elucidated previously. A Hepes buffer molecule bound in the active site may have triggered a conformational change to an active configuration as the two catalytic residues Glu124 and Glu207, together with dependent residues, are observed in a conformation similar to that seen in the structure of Streptomyces lividans CelB2 complexed with an inhibitor. The structural similarity between this cellulase and the mesophilic enzymes serves to highlight features that may be responsible for its thermostability, chiefly an increase in ion pair number and the considerable stabilisation of a mobile region seen in S. lividans CelB2. Additional aromatic residues in the active site region may also contribute to the difference in thermophilicity. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
endoglucanase, Rhodothermus marinus, cellulase, protein structure, thermostability
in
Journal of Molecular Biology
volume
320
issue
4
pages
883 - 897
publisher
Elsevier
external identifiers
  • scopus:0036300754
ISSN
1089-8638
DOI
10.1016/S0022-2836(02)00446-1
language
English
LU publication?
yes
id
2f545f6f-d875-48b3-9691-5bd66220327c (old id 745636)
date added to LUP
2007-12-13 16:05:29
date last changed
2017-01-01 04:25:40
@article{2f545f6f-d875-48b3-9691-5bd66220327c,
  abstract     = {Cellulose is one of the most abundant polysaccharides in nature and microorganisms have developed a comprehensive system for enzymatic breakdown of this ubiquitous carbon source, a subject of much interest in the biotechnology industry. Rhodothermus marinus produces a hyperthermostable cellulase, with a temperature optimum of more than 90 °C, the structure of which is presented here to 1.8 Å resolution. The enzyme has been classified into glycoside hydrolase family 12; this is the first structure of a thermophilic member of this family to have been solved. The β-jelly roll fold observed has identical topology to those of the two mesophilic members of the family whose structures have been elucidated previously. A Hepes buffer molecule bound in the active site may have triggered a conformational change to an active configuration as the two catalytic residues Glu124 and Glu207, together with dependent residues, are observed in a conformation similar to that seen in the structure of Streptomyces lividans CelB2 complexed with an inhibitor. The structural similarity between this cellulase and the mesophilic enzymes serves to highlight features that may be responsible for its thermostability, chiefly an increase in ion pair number and the considerable stabilisation of a mobile region seen in S. lividans CelB2. Additional aromatic residues in the active site region may also contribute to the difference in thermophilicity.},
  author       = {Crennell, Susan and Hreggvidsson, Gudmundur and Nordberg Karlsson, Eva},
  issn         = {1089-8638},
  keyword      = {endoglucanase,Rhodothermus marinus,cellulase,protein structure,thermostability},
  language     = {eng},
  number       = {4},
  pages        = {883--897},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {The structure of Rhodothermus marinus Cel12A, a highly thermostable family 12 endoglucanase, at 1.8 Å resolution},
  url          = {http://dx.doi.org/10.1016/S0022-2836(02)00446-1},
  volume       = {320},
  year         = {2002},
}