2h3e

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{{STRUCTURE_2h3e| PDB=2h3e | SCENE= }}
{{STRUCTURE_2h3e| PDB=2h3e | SCENE= }}
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'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution'''
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===Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17004708 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17004708}}
==About this Structure==
==About this Structure==
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[[Category: Cooperativity]]
[[Category: Cooperativity]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:49:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:58:41 2008''

Revision as of 06:58, 29 July 2008

Template:STRUCTURE 2h3e

Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution

Template:ABSTRACT PUBMED 17004708

About this Structure

2H3E is a Protein complex structure of sequences from Escherichia coli. 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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