2at2
From Proteopedia
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| - | [[Image:2at2.jpg|left|200px]] | + | [[Image:2at2.jpg|left|200px]] |
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| - | '''MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2at2 |SIZE=350|CAPTION= <scene name='initialview01'>2at2</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2AT2 is a [ | + | 2AT2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AT2 OCA]. |
==Reference== | ==Reference== | ||
| - | Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution., Stevens RC, Reinisch KM, Lipscomb WN, Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6087-91. PMID:[http:// | + | Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution., Stevens RC, Reinisch KM, Lipscomb WN, Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6087-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1906175 1906175] |
[[Category: Aspartate carbamoyltransferase]] | [[Category: Aspartate carbamoyltransferase]] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 15:53:33 2008'' |
Revision as of 13:53, 20 March 2008
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| , resolution 3.0Å | |||||||
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| Activity: | Aspartate carbamoyltransferase, with EC number 2.1.3.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of Bacillus subtilis aspartate transcarbamoylase (ATCase; aspartate carbamoyltransferase; carbamoyl-phosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) has been solved by the molecular replacement method at 3.0 A resolution and refined to a crystallographic R factor of 0.19. The enzyme crystallizes in the space group C2 with unit cell dimensions a = 258.5, b = 153.2, and c = 51.9 A and beta = 97.7 degrees. The asymmetric unit is composed of three monomers related by noncrystallographic threefold symmetry. A total of 295 of 304 amino acid residues have been built into the monomer. The last 9 residues in the C terminus were not included in the final model. Each monomer consists of 34% alpha-helix and 18% beta-strand. Three solvent-exposed loop regions (residues 69-84, 178-191, and 212-229) are not well defined in terms of electron density. The catalytic trimer of ATCase from B. subtilis shows great similarity to the catalytic trimer in Escherichia coli ATCase, which was used in constructing the model for molecular replacement. The unliganded trimer from B. subtilis, which is not cooperative, resembles the T (inactive) state slightly more than the R (active)-state form of the E. coli trimer. However, certain regions in the B. subtilis trimer exhibit shifts toward the E. coli R-state conformation.
About this Structure
2AT2 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution., Stevens RC, Reinisch KM, Lipscomb WN, Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6087-91. PMID:1906175
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