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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/745636
- author
- Crennell, Susan
; Hreggvidsson, Gudmundur
and Nordberg Karlsson, Eva
LU
- organization
- publishing date
- 2002
- 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
- 2016-04-01 11:40:17
- date last changed
- 2022-01-26 08:28:09
@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}},
keywords = {{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}},
doi = {{10.1016/S0022-2836(02)00446-1}},
volume = {{320}},
year = {{2002}},
}