1tu0
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1tu0.jpg|left|200px]] | [[Image:1tu0.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1tu0", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | + | --> | |
- | + | {{STRUCTURE_1tu0| PDB=1tu0 | SCENE= }} | |
- | + | ||
- | + | ||
- | }} | + | |
'''Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide''' | '''Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide''' | ||
Line 30: | Line 27: | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
[[Category: Stieglitz, K.]] | [[Category: Stieglitz, K.]] | ||
- | [[Category: | + | [[Category: Allosteric transition]] |
- | [[Category: | + | [[Category: Domain closure]] |
- | [[Category: | + | [[Category: Protein structure-function]] |
- | [[Category: | + | [[Category: Site-specific mutagenesis]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:21:41 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:21, 3 May 2008
Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide
Overview
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 Escherichia coli. Full crystallographic information is available from 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:15288791 Page seeded by OCA on Sat May 3 10:21:41 2008