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1r0c
From Proteopedia
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| - | [[Image:1r0c.jpg|left|200px]] | + | [[Image:1r0c.jpg|left|200px]] |
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| - | '''Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme''' | + | {{Structure |
| + | |PDB= 1r0c |SIZE=350|CAPTION= <scene name='initialview01'>1r0c</scene>, resolution 2.37Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=NCD:N-CARBAMOYL-L-ASPARTATE'>NCD</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 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]) | ||
| + | }} | ||
| + | |||
| + | '''Products in the T State of Aspartate Transcarbamylase: Crystal Structure of the Phosphate and N-carbamyl-L-aspartate Ligated Enzyme''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R0C is a [ | + | 1R0C 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=1R0C OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15157076 15157076] |
[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: n-carbamyl-l-aspartate(cla)]] | [[Category: n-carbamyl-l-aspartate(cla)]] | ||
[[Category: phosphate]] | [[Category: phosphate]] | ||
| - | [[Category: | + | [[Category: product]] |
[[Category: t state]] | [[Category: t state]] | ||
| - | ''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 13:45:07 2008'' |
Revision as of 11:45, 20 March 2008
| |||||||
| , resolution 2.37Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| 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 | ||||||
| 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
Overview
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 Structure
1R0C is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:45:07 2008
