2nt8
From Proteopedia
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ATP bound at the active site of a PduO type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri
Overview
The three-dimensional crystal structure of the PduO-type corrinoid, adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to, 1.68-A resolution. The functional assignment of LrPduO as a corrinoid, adenosyltransferase was confirmed by in vivo and in vitro evidence. The, enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13, microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with, Mg-ATP resulted in well-defined electron density for an N-terminal loop, that had been disordered in other PduO-type enzyme structures. This newly, defined N-terminal loop makes up the lower portion of the enzyme active, site with the other half being contributed from an adjacent subunit. These, results provide the first detailed description of the enzyme active site, for a PduO-type adenosyltransferase and identify a unique ATP binding, motif at the protein N terminus. The molecular architecture at the active, site offers valuable new insight into the role of various residues, responsible for the human disease methylmalonic aciduria.
About this Structure
2NT8 is a Single protein structure of sequence from Lactobacillus reuteri with , , and as ligands. Active as Cob(I)yrinic acid a,c-diamide adenosyltransferase, with EC number 2.5.1.17 Full crystallographic information is available from OCA.
Reference
Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri., St Maurice M, Mera PE, Taranto MP, Sesma F, Escalante-Semerena JC, Rayment I, J Biol Chem. 2007 Jan 26;282(4):2596-605. Epub 2006 Nov 22. PMID:17121823
Page seeded by OCA on Wed Jan 23 15:24:32 2008
