Linked Life Data

9772161

Source:http://linkedlifedata.com/resource/pubmed/id/9772161

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1998-11-3
pubmed:databankReference
pubmed:abstractText
The structure of (D)-glucarate dehydratase from Pseudomonas putida (GlucD) has been solved at 2.3 A resolution by multiple isomorphous replacement and refined to a final R-factor of 19.0%. The protein crystallizes in the space group I222 with one subunit in the asymmetric unit. The unit cell dimensions are a = 69.6 A, b = 108.8 A, and c = 122.6 A. The crystals were grown using the batch method where the primary precipitant was poly(ethylene glycol) 1000. The structure reveals that GlucD is a tetramer of four identical polypeptides, each containing 451 residues. The structure was determined without a bound substrate or substrate analogue. Three disordered regions are noted: the N-terminus through residue 11, a loop containing residues 99 through 110, and the C-terminus from residue 423. On the basis of primary sequence alignments, we previously concluded that GlucD is a member of the mandelate racemase (MR) subfamily of the enolase superfamily [Babbitt, P. C., Hasson, M. S., Wedekind, J. E., Palmer, D. R. J., Barrett, W. C., Reed, G. J., Rayment, I., Ringe, D., Kenyon, G. L., and Gerlt, J. A. (1996) Biochemistry 35, 16489-16501]. This prediction is now verified, since the overall fold of GlucD is strikingly similar to those of MR, muconate lactonizing enzyme I, and enolase. Also, many of the active site residues of GlucD can be superimposed on those found in the active site of MR. The implications of this structure on the evolution of catalysis in the enolase superfamily are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14358-68
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9772161-Amino Acid Sequence, pubmed-meshheading:9772161-Crystallization, pubmed-meshheading:9772161-Crystallography, X-Ray, pubmed-meshheading:9772161-Enzyme Activation, pubmed-meshheading:9772161-Evolution, Molecular, pubmed-meshheading:9772161-Hydro-Lyases, pubmed-meshheading:9772161-Models, Molecular, pubmed-meshheading:9772161-Molecular Sequence Data, pubmed-meshheading:9772161-Peptide Fragments, pubmed-meshheading:9772161-Phosphopyruvate Hydratase, pubmed-meshheading:9772161-Protein Structure, Secondary, pubmed-meshheading:9772161-Protein Structure, Tertiary, pubmed-meshheading:9772161-Pseudomonas putida, pubmed-meshheading:9772161-Racemases and Epimerases, pubmed-meshheading:9772161-Sequence Alignment, pubmed-meshheading:9772161-Sequence Homology, Amino Acid, pubmed-meshheading:9772161-Structure-Activity Relationship
pubmed:year
1998
pubmed:articleTitle
Evolution of enzymatic activities in the enolase superfamily: crystal structure of (D)-glucarate dehydratase from Pseudomonas putida.
pubmed:affiliation
The Institute for Enzyme Research, Department of Biochemistry, University of Wisconsin, Madison 53706, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.