1nht
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ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K
OverviewOverview
Crystal structures of adenylosuccinate synthetase from Escherichia coli, complexed with Mg2+, 6-thiophosphoryl-IMP, GDP, and hadacidin at 298 and, 100 K have been refined to R-factors of 0.171 and 0.206 against data to, 2.8 and 2.5 A resolution, respectively. Interactions of GDP, Mg2+ and, hadacidin are similar to those observed for the same ligands in the, complex of IMP, GDP, NO3-, Mg2+ and hadacidin (Poland, B. W., Fromm, H. J., & Honzatko, R. B. (1996). J. Mol. Biol. 264, 1013-1027). Although crystals, were grown from solutions containing 6-mercapto-IMP and GTP, the electron, density at the active site is consistent with 6-thiophosphoryl-IMP and, GDP. Asp-13 and Gln-224 probably work in concert to stabilize the, 6-thioanion of 6-mercapto-IMP, which in turn is the nucleophile in ... [(full description)]
About this StructureAbout this Structure
1NHT is a [Single protein] structure of sequence from [Escherichia coli] with MG, GDP, HAD and PGS as [ligands]. Active as [[1]], with EC number [6.3.4.4]. Full crystallographic information is available from [OCA].
ReferenceReference
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli., Poland BW, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1997 Jun 13;272(24):15200-5. PMID:9182542
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