Linked Life Data

18662315

Source:http://linkedlifedata.com/resource/pubmed/id/18662315

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-9-15
pubmed:abstractText
We have modelled, using the CHARMM27 energy force field, the structures of closed and open forms of Staphylococcus simulans lipase (SSL) on the basis of the crystal structures of Bacillus stearothermophilus and Staphylococcus hyicus lipases, respectively. The models suggested the presence of a main lid and a second lid that may act with the former as a double door to control the access to the active site. Superimposition of both closed and open forms of SSL allowed us to determine the hinge regions allowing the movements of the main and the second lid upon lipase activation. The flexibility of these hinge regions was checked by molecular dynamics simulations. The SSL models also allowed us to identify key residues involved in binding substrates, calcium or zinc ions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:volume
286
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
207-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
3-D structure modelling of the Staphylococcus simulans lipase: conformational changes, substrate specificity and novel structural features.
pubmed:affiliation
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS route Soukra, Sfax-Tunisia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't