Linked Life Data

11565853

Source:http://linkedlifedata.com/resource/pubmed/id/11565853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-9-21
pubmed:abstractText
The three-dimensional structure of thermostable catechol 2,3-dioxygenase(TC230) from Bacillus Stearothermophilus has been modeled basing on the known x-ray structure of catechol 2,3-dioxygenase(metapyrocatechase) from Pseudomonas putida mt-2, using computer graphics energy minimization techniques. The rationality of the resulting model was validated by Ramachandran plot and Profile-3D. The structure-functionally important residues, such as M++ binding residues and the substrate binding residues, were identified from the model. These residues are candidates for further site-directed mutagenesis experiments. The reason that the thermostability of TC230 is greater than metapyrocatechase(MPC) has been found, which may be due to the specific structure of the TC230 in the C-end mainly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0739-1102
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-83
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Modeling and analysis of the structure of the thermostable catechol 2,3-dioxygenase from Bacillus Stearothermophilus.
pubmed:affiliation
Center of Analysis and Measurement, School of Life Sciences, Fudan University, Shanghai, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't