Linked Life Data

20609364

Source:http://linkedlifedata.com/resource/pubmed/id/20609364

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2010-8-2
pubmed:abstractText
Cel9A from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius belongs to the subfamily E1 of family 9 glycoside hydrolases, many members of which have an N-terminal Ig-like domain followed by the catalytic domain. The Ig-like domain is not directly involved in either carbohydrate binding or biocatalysis; however, deletion of the Ig-domain promotes loss of enzymatic activity. We have investigated the functional role of the Ig-like domain using molecular dynamics simulations. Our simulations indicate that residues within the Ig-like domain are dynamically correlated with residues in the carbohydrate-binding pocket and with key catalytic residues of Cel9A. Free energy perturbation simulations indicate that the Ig-like domain stabilizes the catalytic domain and may be responsible for the enhanced thermostability of Cel9A.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1873-3468
pubmed:author
pubmed:issnType
Electronic
pubmed:day
4
pubmed:volume
584
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3431-5
pubmed:dateRevised
2010-10-25
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A.
pubmed:affiliation
Deconstruction Division, Joint BioEnergy Institute, Emeryville, CA, United States.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.