2h3e
From Proteopedia
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|PDB= 2h3e |SIZE=350|CAPTION= <scene name='initialview01'>2h3e</scene>, resolution 2.300Å | |PDB= 2h3e |SIZE=350|CAPTION= <scene name='initialview01'>2h3e</scene>, resolution 2.300Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=6PR:(S)-4-AMINO-4-OXO-3-(2-PHOSPHONOACETAMIDO)BUTANOIC+ACID'>6PR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d09|1D09]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3e OCA], [http://www.ebi.ac.uk/pdbsum/2h3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h3e RCSB]</span> | ||
}} | }} | ||
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[[Category: Tsuruta, H.]] | [[Category: Tsuruta, H.]] | ||
[[Category: Xia, J.]] | [[Category: Xia, J.]] | ||
| - | [[Category: 6PR]] | ||
| - | [[Category: ZN]] | ||
[[Category: cooperativity]] | [[Category: cooperativity]] | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:54 2008'' |
Revision as of 00:24, 31 March 2008
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| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | pyrB (Escherichia coli), pyrI (Escherichia coli) | ||||||
| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Related: | 1D09
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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. 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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