Linked Life Data

9705652

Source:http://linkedlifedata.com/resource/pubmed/id/9705652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-8-12
pubmed:databankReference
pubmed:abstractText
The phosphoenolpyruvate:sugar phosphotransferase system (PTS) is a bacterial and mycoplasma system responsible for the uptake of some sugars, concomitant with their phosphorylation. The sugar-specific component of the system, enzyme II (EII),consists of three domains, EIIA, EIIB and EIIC. EIIA and ELLB are cytoplasmic and EIIC is an integral membrane protein that contains the sugar-binding site. Phosphoenolpyruvate (PEP) provides the source of the phosphoryl group, which is transferred via several phosphoprotein intermediates, eventually being transferred to the internalized sugar. Along the pathway, EIIA accepts a phosphoryl group from the phosphocarrier protein HPr and transfers it to EIIB. The structure of the glucose-specific EIIA (EIIAglc) from Mycoplasma capricolum reported here facilitates understanding of the nature of the interactions between this protein and its partners.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
697-710
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A promiscuous binding surface: crystal structure of the IIA domain of the glucose-specific permease from Mycoplasma capricolum.
pubmed:affiliation
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.