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[[Image:1tth.gif|left|200px]]


{{Structure
==Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA)==
|PDB= 1tth |SIZE=350|CAPTION= <scene name='initialview01'>1tth</scene>, resolution 2.80&Aring;
<StructureSection load='1tth' size='340' side='right'caption='[[1tth]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC ACID'>PAL</scene>
<table><tr><td colspan='2'>[[1tth]] 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=1TTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TTH FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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=PAL:N-(PHOSPHONACETYL)-L-ASPARTIC+ACID'>PAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tth OCA], [https://pdbe.org/1tth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tth RCSB], [https://www.ebi.ac.uk/pdbsum/1tth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tth 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/tt/1tth_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=1tth ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA)'''
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:15288791<ref>PMID:15288791</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tth" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1TTH 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=1TTH OCA].
__TOC__
 
</StructureSection>
==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: PAL]]
[[Category: ZN]]
[[Category: allosteric transition]]
[[Category: domain closure]]
[[Category: site-specific mutagenesis]]
 
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Retrieved from "https://proteopedia.org/1tth"