2h3e
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(New page: 200px<br /><applet load="2h3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h3e, resolution 2.300Å" /> '''Structure of wild-t...)
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Revision as of 09:24, 21 November 2007
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Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution
Overview
The synthesis of a new inhibitor, N-phosphonacetyl-L-isoasparagine (PALI), of Escherichia coli aspartate transcarbamoylase (ATCase) is reported, as, well as structural studies of the enzyme.PALI complex. PALI was, synthesized in 7 steps from beta-benzyl L-aspartate. The KD of PALI was 2, microM. Kinetics and small-angle X-ray scattering experiments showed that, PALI can induce the cooperative transition of ATCase from the T to the R, state. The X-ray structure of the enzyme.PALI complex showed 22, hydrogen-bonding interactions between the enzyme and PALI. The kinetic, characterization and crystal structure of the ATCase.PALI complex also, provides detailed information regarding the importance of the, alpha-carboxylate for the binding of the substrate aspartate.
About this Structure
2H3E is a Protein complex structure of sequences from Escherichia coli with ZN and 6PR as ligands. Active as Aspartate carbamoyltransferase, with EC number 2.1.3.2 Full crystallographic information is available from OCA.
Reference
N-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase., Eldo J, Cardia JP, O'Day EM, Xia J, Tsuruta H, Kantrowitz ER, J Med Chem. 2006 Oct 5;49(20):5932-8. PMID:17004708
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