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| - | [[Image:1d09.gif|left|200px]] | |
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| - | <!--
| + | ==ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)== |
| - | The line below this paragraph, containing "STRUCTURE_1d09", creates the "Structure Box" on the page.
| + | <StructureSection load='1d09' size='340' side='right'caption='[[1d09]], [[Resolution|resolution]] 2.10Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1d09]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D09 FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | {{STRUCTURE_1d09| PDB=1d09 | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d09 OCA], [https://pdbe.org/1d09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d09 RCSB], [https://www.ebi.ac.uk/pdbsum/1d09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d09 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PYRB_ECOLI PYRB_ECOLI] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d0/1d09_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </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=1d09 ConSurf]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)'''
| + | ==See Also== |
| - | | + | *[[Aspartate carbamoyltransferase|Aspartate carbamoyltransferase]] |
| - | | + | *[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]] |
| - | ==Overview== | + | __TOC__ |
| - | A high-resolution structure of Escherichia coli aspartate transcarbamoylase has been determined to 2.1 A; resolution in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate (PALA). The structure was refined to a free R-factor of 23.4% and a working R-factor of 20.3%. The PALA molecule is completely saturated with interactions to side chain and backbone groups in the active site, including two interactions that are contributed from the 80s loop of the adjacent catalytic chain. The charge neutralization of the bound PALA molecule (and presumably the substrates as well) induced by the electrostatic field of the highly positively charged active site is an important factor in the high binding affinity of PALA and must be important for catalysis. The higher-resolution structure reported here departs in a number of ways from the previously determined structure at lower resolution. These modifications include alterations in the backbone conformation of the C-terminal of the catalytic chains, the N- and C-termini of the regulatory chains, and two loops of the regulatory chain. The high-resolution of this structure has allowed a more detailed description of the binding of PALA to the active site of the enzyme and has allowed a detailed model of the tetrahedral intermediate to be constructed. This model becomes the basis of a description of the catalytic mechanism of the transcarbamoylase reaction. The R-structural state of the enzyme-PALA complex is an excellent representation of the form of the enzyme that occurs at the moment in the catalytic cycle when the tetrahedral intermediate is formed. Finally, improved electron density in the N-terminal region of the regulatory chain (residues 1 to 7) has allowed tracing of the entire regulatory chain. The N-terminal segments of the R1 and R6 chains are located in close proximity to each other and to the regulatory site. This portion of the molecule may be involved in the observed asymmetry between the regulatory binding sites as well as in the heterotropic response of the enzyme.
| + | </StructureSection> |
| - | | + | |
| - | ==About this Structure==
| + | |
| - | 1D09 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=1D09 OCA].
| + | |
| - | | + | |
| - | ==Reference==
| + | |
| - | Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A., Jin L, Stec B, Lipscomb WN, Kantrowitz ER, Proteins. 1999 Dec 1;37(4):729-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10651286 10651286]
| + | |
| - | [[Category: Aspartate carbamoyltransferase]] | + | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Protein complex]] | + | [[Category: Large Structures]] |
| - | [[Category: Jin, L.]] | + | [[Category: Jin L]] |
| - | [[Category: Kantrowitz, E R.]] | + | [[Category: Kantrowitz ER]] |
| - | [[Category: Lipscomb, W N.]] | + | [[Category: Lipscomb WN]] |
| - | [[Category: Stec, B.]] | + | [[Category: Stec B]] |
| - | [[Category: Protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:18:04 2008''
| + | |
