Linked Life Data

11846565

Source:http://linkedlifedata.com/resource/pubmed/id/11846565

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2002-2-15
pubmed:databankReference
pubmed:abstractText
Here, we report the first crystal structure of a photosynthetic glyceraldehyde-3-phosphate dehydrogenase (GAPDH) complexed with NADP. The enzyme, purified from spinach chloroplasts, is constituted of a single type of subunit (A) arranged in homotetramers. It shows non-regulated NADP-dependent and NAD-dependent activities, with a preference for NADP. The structure has been solved to 3.0 A resolution by molecular replacement. The crystals belong to space group C222 with three monomers in the asymmetric unit. One of the three monomers generates a tetramer using the space group 222 point symmetry and a very similar tetramer is generated by the other two monomers, related by a non-crystallographic symmetry, using a crystallographic 2-fold axis. The protein reveals a large structural homology with known GAPDHs both in the cofactor-binding domain and in regions of the catalytic domain. Like all other GAPDHs investigated so far, the A(4)-GAPDH belongs to the Rossmann fold family of dehydrogenases. However, unlike most dehydrogenases of this family, the adenosine 2'-phosphate group of NADP does not form a salt-bridge with any positively charged residue in its surroundings, being instead set in place by hydrogen bonds with a threonine residue belonging to the Rossmann fold and a serine residue located in the S-loop of a symmetry-related monomer. While increasing our knowledge of an important photosynthetic enzyme, these results contribute to a general understanding of NADP versus NAD recognition in pyridine nucleotide-dependent enzymes. Although the overall structure of A(4)-GAPDH is similar to that of the cytosolic GAPDH from bacteria and eukaryotes, the chloroplast tetramer is peculiar, in that it can actually be considered a dimer of dimers, since monomers are bound in pairs by a disulphide bridge formed across Cys200 residues. This bridge is not found in other cytosolic or chloroplast GAPDHs from animals, bacteria, or plants other than spinach.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
314
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
527-42
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11846565-Amino Acid Sequence, pubmed-meshheading:11846565-Binding Sites, pubmed-meshheading:11846565-Catalytic Domain, pubmed-meshheading:11846565-Crystallography, X-Ray, pubmed-meshheading:11846565-Geobacillus stearothermophilus, pubmed-meshheading:11846565-Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+), pubmed-meshheading:11846565-Hydrogen Bonding, pubmed-meshheading:11846565-Isoenzymes, pubmed-meshheading:11846565-Models, Molecular, pubmed-meshheading:11846565-Molecular Sequence Data, pubmed-meshheading:11846565-NADP, pubmed-meshheading:11846565-Protein Structure, Quaternary, pubmed-meshheading:11846565-Protein Structure, Tertiary, pubmed-meshheading:11846565-Sequence Alignment, pubmed-meshheading:11846565-Spinacia oleracea, pubmed-meshheading:11846565-Static Electricity, pubmed-meshheading:11846565-Sulfates, pubmed-meshheading:11846565-Water
pubmed:year
2001
pubmed:articleTitle
Crystal structure of the non-regulatory A(4 )isoform of spinach chloroplast glyceraldehyde-3-phosphate dehydrogenase complexed with NADP.
pubmed:affiliation
Dipartimento di Chimica "G. Ciamician", Università di Bologna, via Selmi 2, Bologna, 40126, Italia. fermani@ciam.unibo.it
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't