Linked Life Data

15182170

Source:http://linkedlifedata.com/resource/pubmed/id/15182170

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2004-6-8
pubmed:abstractText
The structure and dynamic properties of the C-terminal region of the human class alpha glutathione transferase A1-1 have been investigated with high-resolution NMR methods. On the basis of crystallographic and fluorescence measurements, this 13-residue segment of the enzyme is presumed to be disordered in the unliganded enzyme. When the product or product analogue is bound, a C-terminal alpha-helix is observed in crystal structures. Conflicting data exists regarding the structure of this region when one of the substrates, glutathione (GSH), is bound. The NMR studies presented here show that in the unliganded protein, this region of the protein samples different conformations, most likely an ensemble of helix-like structures. Addition of either GSH or the conjugate between GSH and ethacrynic acid (EASG) causes this segment to become a stable alpha-helix. In the GSH complex, the ends of this helix exhibit dynamic behavior on both the millisecond and nanosecond time scales. In contrast, there is no evidence of millisecond dynamics in the EASG complex. The ligand-induced ordering of the enzyme reduces the intrinsic affinity of the enzyme for its product, facilitating enzymatic turnover.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7244-54
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Glutathione induces helical formation in the carboxy terminus of human glutathione transferase A1-1.
pubmed:affiliation
Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't