1ecb: Difference between revisions
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Revision as of 16:05, 30 October 2007
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ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE COMPLEXED WITH 2 GMP, 1 MG PER SUBUNIT
OverviewOverview
Activation of gluatmine phosphoribosylpyrophosphate (RPPP), amidotransferase (GPATase) by binding of a PRPP substrate analog results, in the formation of a 20 A channel connecting the active site for, glutamine hydrolysis in one domain with the PRPP site in a second domain., This solvent-inaccessible channel permits transfer of the NH3 intermediate, between the two active sites. Tunneling of NH3 may be a common mechanism, for glutamine amidotransferase-catalyzed nitrogen transfer and for, coordination of catalysis at two distinct active sites in complex enzymes., The 2.4 A crystal structure of the active conformer of GPATase also, provides the first description of an intact active site for the, phosphoribosyltransferase (PRTase) family of nucleotide synthesis and, salvage enzymes. ... [(full description)]
About this StructureAbout this Structure
1ECB is a [Single protein] structure of sequence from [Escherichia coli] with MG and 5GP as [ligands]. Active as [Amidophosphoribosyltransferase], with EC number [2.4.2.14]. Structure known Active Sites: NTA, NTB, NTC, NTD, PRA, PRB, PRC and PRT. Full crystallographic information is available from [OCA].
ReferenceReference
Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site., Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL, Biochemistry. 1997 Sep 16;36(37):11061-8. PMID:9333323
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