1r0c: Difference between revisions
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|PDB= 1r0c |SIZE=350|CAPTION= <scene name='initialview01'>1r0c</scene>, resolution 2.37Å | |PDB= 1r0c |SIZE=350|CAPTION= <scene name='initialview01'>1r0c</scene>, resolution 2.37Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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 OR B4245 OR C5345 OR Z5856 OR ECS5222 OR SF4245 OR S4507 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), PYRI OR B4244 OR C5344 OR Z5855 OR ECS5221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= PYRB OR B4245 OR C5345 OR Z5856 OR ECS5222 OR SF4245 OR S4507 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), PYRI OR B4244 OR C5344 OR Z5855 OR ECS5221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1r0b|1R0B]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0c OCA], [http://www.ebi.ac.uk/pdbsum/1r0c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r0c RCSB]</span> | |||
}} | }} | ||
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[[Category: Huang, J.]] | [[Category: Huang, J.]] | ||
[[Category: Lipscomb, W N.]] | [[Category: Lipscomb, W N.]] | ||
[[Category: aspartate carbamoyltransferase]] | [[Category: aspartate carbamoyltransferase]] | ||
[[Category: aspartate transcarbamylase]] | [[Category: aspartate transcarbamylase]] | ||
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[[Category: t state]] | [[Category: t state]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:27 2008'' | ||
Revision as of 23:21, 30 March 2008
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| , resolution 2.37Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | PYRB OR B4245 OR C5345 OR Z5856 OR ECS5222 OR SF4245 OR S4507 (Escherichia coli), PYRI OR B4244 OR C5344 OR Z5855 OR ECS5221 (Escherichia coli) | ||||||
| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Related: | 1R0B
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme
OverviewOverview
The structure of aspartate transcarbamylase of Escherichia coli ligated to products (phosphate and N-carbamyl-l-aspartate) has been determined at 2.37 A resolution (R-factor = 0.23, R(free) = 0.27). Results might indicate a product release mode, rather than close analogues to the transition state like those found in our earlier studies of other ligands (N-phosphonacetyl-L-aspartate, carbamyl phosphate plus malonate, phosphonoacetamide plus malonate, or citrate plus phosphate). Ordered product release, first carbamylaspartate (CLA) and then phosphate, might be facilitated by a 4 A movement of phosphate from the substrate-analogue position to the product (phosphate) binding position, and by a somewhat similar release movement of the other product (CLA) relative to its analogue (citrate). This movement is consistent with earlier studies of binding of either pyrophosphate or phosphate alone [Honzatko, R. B., and Lipscomb, W. N. (1982) J. Mol. Biol. 160, 265-286].
About this StructureAbout this Structure
1R0C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-L-aspartate ligated enzyme., Huang J, Lipscomb WN, Biochemistry. 2004 Jun 1;43(21):6422-6. PMID:15157076
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