This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1tug

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1tug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tug, resolution 2.10&Aring;" /> '''Aspartate Transcarba...)
Current revision (06:15, 3 April 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tug.jpg|left|200px]]<br /><applet load="1tug" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1tug, resolution 2.10&Aring;" />
 
-
'''Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP)'''<br />
 
-
==Overview==
+
==Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP)==
-
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.
+
<StructureSection load='1tug' size='340' side='right'caption='[[1tug]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1tug]] 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=1TUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUG FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=PCT:PHOSPHONOACETAMIDE'>PCT</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=1tug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tug OCA], [https://pdbe.org/1tug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tug RCSB], [https://www.ebi.ac.uk/pdbsum/1tug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tug 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/tu/1tug_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=1tug ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1TUG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, MLI, PCT and CTP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TUG OCA].
+
*[[Aspartate carbamoyltransferase 3D structures|Aspartate carbamoyltransferase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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: CTP]]
+
-
[[Category: MLI]]
+
-
[[Category: PCT]]
+
-
[[Category: ZN]]
+
-
[[Category: allosteric transition]]
+
-
[[Category: domain closure]]
+
-
[[Category: protein structure-function]]
+
-
[[Category: site specific mutagenesis]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:36:08 2007''
+

Current revision

Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP)

PDB ID 1tug

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tug"
Personal tools