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2at2

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[[Image:2at2.jpg|left|200px]]
 
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{{Structure
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==MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION==
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|PDB= 2at2 |SIZE=350|CAPTION= <scene name='initialview01'>2at2</scene>, resolution 3.0&Aring;
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<StructureSection load='2at2' size='340' side='right'caption='[[2at2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2at2]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AT2 FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2at2 OCA], [https://pdbe.org/2at2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2at2 RCSB], [https://www.ebi.ac.uk/pdbsum/2at2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2at2 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2at2 OCA], [http://www.ebi.ac.uk/pdbsum/2at2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2at2 RCSB]</span>
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[https://www.uniprot.org/uniprot/PYRB_BACSU PYRB_BACSU]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/at/2at2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2at2 ConSurf].
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<div style="clear:both"></div>
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'''MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Aspartate carbamoyltransferase]]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lipscomb, W N.]]
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[[Category: Lipscomb WN]]
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[[Category: Reinisch, K M.]]
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[[Category: Reinisch KM]]
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[[Category: Stevens, R C.]]
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[[Category: Stevens RC]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:57 2008''
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Current revision

MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION

PDB ID 2at2

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