Linked Life Data

17242513

Source:http://linkedlifedata.com/resource/pubmed/id/17242513

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2007-1-23
pubmed:databankReference
pubmed:abstractText
Salmonella typhimurium YeaD (stYeaD), annotated as a putative aldose 1-epimerase, has a very low sequence identity to other well characterized mutarotases. Sequence analysis suggested that the catalytic residues and a few of the substrate-binding residues of galactose mutarotases (GalMs) are conserved in stYeaD. Determination of the crystal structure of stYeaD in an orthorhombic form at 1.9 A resolution and in a monoclinic form at 2.5 A resolution revealed this protein to adopt the beta-sandwich fold similar to GalMs. Structural comparison of stYeaD with GalMs has permitted the identification of residues involved in catalysis and substrate binding. In spite of the similar fold and conservation of catalytic residues, minor but significant differences were observed in the substrate-binding pocket. These analyses pointed out the possible role of Arg74 and Arg99, found only in YeaD-like proteins, in ligand anchoring and suggested that the specificity of stYeaD may be distinct from those of GalMs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-205
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases.
pubmed:affiliation
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't