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[[Image:1tu0.jpg|left|200px]]


{{Structure
==Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide==
|PDB= 1tu0 |SIZE=350|CAPTION= <scene name='initialview01'>1tu0</scene>, resolution 2.55&Aring;
<StructureSection load='1tu0' size='340' side='right'caption='[[1tu0]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PCT:PHOSPHONOACETAMIDE'>PCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[1tu0]] 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=1TU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TU0 FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
|GENE= PYRB, B4245, C5345, Z5856, ECS5222, SF4245, S4507 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), PYRI, B4244, C5344, Z5855, ECS5221 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCT:PHOSPHONOACETAMIDE'>PCT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu0 OCA], [https://pdbe.org/1tu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu0 ProSAT]</span></td></tr>
|RELATEDENTRY=[[3at1|3AT1]], [[1tth|1TTH]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu0 OCA], [http://www.ebi.ac.uk/pdbsum/1tu0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tu0 RCSB]</span>
== 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/tu/1tu0_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=1tu0 ConSurf].
<div style="clear:both"></div>


'''Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide'''
==See Also==
 
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
A detailed description of the transition that allosteric enzymes undergo constitutes a major challenge in structural biology. We have succeeded in trapping four distinct allosteric states of a mutant enzyme of Escherichia coli aspartate transcarbomylase and determining their structures by X-ray crystallography. The mutant version of aspartate transcarbamoylase in which Glu50 in the catalytic chains was replaced by Ala destabilizes the native R state and shifts the equilibrium towards the T state. This behavior allowed the use of substrate analogs such as phosphonoacetamide and malonate to trap the enzyme in T-like and R-like structures that are distinct from the T-state structure of the wild-type enzyme (as represented by the structure of the enzyme with CTP bound and the R-state structure as represented by the structure with N-(phosphonacetyl)-L-aspartate bound). These structures shed light on the nature and the order of internal structural rearrangements during the transition from the T to the R state. They also suggest an explanation for diminished activity of the E50A enzyme and for the change in reaction mechanism from ordered to random for this mutant enzyme.
 
==About this Structure==
1TU0 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=1TU0 OCA].
 
==Reference==
Monitoring the transition from the T to the R state in E.coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant enzyme in four distinct allosteric states., Stieglitz K, Stec B, Baker DP, Kantrowitz ER, J Mol Biol. 2004 Aug 13;341(3):853-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15288791 15288791]
[[Category: Aspartate carbamoyltransferase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Baker, D P.]]
[[Category: Baker DP]]
[[Category: Kantrowitz, E R.]]
[[Category: Kantrowitz ER]]
[[Category: Stec, B.]]
[[Category: Stec B]]
[[Category: Stieglitz, K.]]
[[Category: Stieglitz K]]
[[Category: allosteric transition]]
[[Category: domain closure]]
[[Category: protein structure-function]]
[[Category: site-specific mutagenesis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:02 2008''
Retrieved from "https://proteopedia.org/1tu0"