1o17
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(New page: 200px<br /><applet load="1o17" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o17, resolution 2.05Å" /> '''ANTHRANILATE PHOSPHO...)
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Revision as of 20:35, 20 November 2007
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ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)
Overview
The crystal structure of the dimeric anthranilate, phosphoribosyltransferase (AnPRT) reveals a new category of, phosphoribosyltransferases, designated as class III. The active site of, this enzyme is located within the flexible hinge region of its two-domain, structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is, co-ordinated by a metal ion and is bound by two conserved loop regions, within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan, biosynthesis pathway is complete, thereby connecting the evolution of its, enzyme members to the general development of metabolic processes. Its, structure reveals it to have the same fold, topology, active site location, and type of association as class II nucleoside phosphorylases. At the, level of sequences, this relationship is mirrored by 13 structurally, invariant residues common to both enzyme families. Taken together, these, data imply common ancestry of enzymes catalysing reverse biological, processes--the ribosylation and deribosylation of metabolic pathway, intermediates. These relationships establish new links for enzymes, involved in nucleotide and amino acid metabolism.
About this Structure
1O17 is a Single protein structure of sequence from Sulfolobus solfataricus. This structure superseeds the now removed PDB entry 1K8E. Active as Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18 Full crystallographic information is available from OCA.
Reference
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry., Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M, EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726
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