This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1nht
From Proteopedia
|
ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K
Overview
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 Structure
1NHT is a [Single protein] structure of sequence from [Escherichia coli] with MG, GDP, HAD and PGS as [ligands]. Active as [Adenylosuccinate synthase], with EC number [6.3.4.4]. Structure known Active Sites: ASP, GNS and IMP. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 15:43:47 2007
