1tth

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tth.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tth.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tth| PDB=1tth | SCENE= }}
{{STRUCTURE_1tth| PDB=1tth | SCENE= }}
-
'''Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA)'''
+
===Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA)===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15288791}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15288791 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15288791}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Domain closure]]
[[Category: Domain closure]]
[[Category: Site-specific mutagenesis]]
[[Category: Site-specific mutagenesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:20:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:39:06 2008''

Revision as of 04:39, 29 July 2008

Template:STRUCTURE 1tth

Aspartate Transcarbamoylase Catalytic Chain Mutant Glu50Ala Complexed with N-(Phosphonacetyl-L-Aspartate) (PALA)

Template:ABSTRACT PUBMED 15288791

About this Structure

1TTH 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 Tue Jul 29 07:39:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools