Linked Life Data

18540639

Source:http://linkedlifedata.com/resource/pubmed/id/18540639

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
2008-6-24
pubmed:databankReference
pubmed:abstractText
3-Phosphoglycerate kinase is a hinge-bending enzyme with substrate-assisted domain closure. However, the closure mechanism has not been described in terms of structural details. Here we present experimental evidence of the participation of individual substrate binding side chains in the operation of the main hinge which is distant from the substrate binding sites. The combined mutational, kinetic, and structural (DSC and SAXS) data for human 3-phosphoglycerate kinase have shown that catalytic residue R38, which also binds the substrate 3-phosphoglycerate, is essential in inducing domain closure. Similarly, residues K219, N336, and E343 which interact with the nucleotide substrates are involved in the process of domain closure. The other catalytic residue, K215, covers a large distance during catalysis but has no direct role in domain closure. The transmission path of the nucleotide effect toward the main hinge of PGK is described for the first time at the level of interactions existing in the tertiary structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6735-44
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Communication between the nucleotide site and the main molecular hinge of 3-phosphoglycerate kinase.
pubmed:affiliation
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1518 Budapest, PO Box 7, Hungary, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't