2h3e: Difference between revisions
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'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution''' | {{Structure | ||
|PDB= 2h3e |SIZE=350|CAPTION= <scene name='initialview01'>2h3e</scene>, resolution 2.300Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=6PR:(S)-4-AMINO-4-OXO-3-(2-PHOSPHONOACETAMIDO)BUTANOIC ACID'>6PR</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_carbamoyltransferase Aspartate carbamoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.3.2 2.1.3.2] | |||
|GENE= pyrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), pyrI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2H3E is a [ | 2H3E is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H3E OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17004708 17004708] | ||
[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:12:08 2008'' | ||
Revision as of 18:12, 20 March 2008
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| , resolution 2.300Å | |||||||
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| Ligands: | and | ||||||
| Gene: | pyrB (Escherichia coli), pyrI (Escherichia coli) | ||||||
| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of N-phosphonacetyl-L-isoasparagine at 2.3A resolution
OverviewOverview
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 StructureAbout this Structure
2H3E is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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