@article{ref1,
title="A new metal-binding site for yeast phosphoglycerate kinase as determined by the use of a metal-ATP analog",
journal="Biophysical journal",
year="1997",
author="Pappu, K. M. and Kunnumal, B. and Serpersu, E. H.",
volume="72",
number="2 Pt 1",
pages="928-935",
abstract="Suicide substrate beta, gamma-bidentate Rh(III)ATP (RhATP) was used to map the metal ion-binding site in yeast phosphoglycerate kinase (PGK). Cleavage of the RhATP-inactivated enzyme with pepsin and subsequent separation of peptides by reverse-phase high-performance liquid chromatography gave two Rh-nucleotide bound peptides. One of the peptides corresponded to the C-terminal residues of PGK, and the other to a part of helix V. Of the four glutamates present in the C-terminal peptide, Glu 398 may be a likely metal coordination site. Therefore, importance of the C-terminal residues in PGK catalysis may be attributed, in part to the coordination of metal ion of the metal-ATP substrate. Metal coordination may then align the C-terminal peptide to extend toward the N-terminal domain and form the &quot;closed&quot; active site. <br><br>RESULTS presented in this paper suggest that one or more side chains of the enzyme may be coordinated to the metal ion in the PGK.3-phospho-D-glycerate-RhATP complex, and that exchange-inert metal-ATP analogs could be used to determine metal coordination sites on kinases and other metal-ATP-utilizing enzymes.<p /><p>Language: en</p>",
language="en",
issn="0006-3495",
doi="10.1016/s0006-3495(97)78726-5",
url="http://dx.doi.org/10.1016/s0006-3495(97)78726-5"
}