3c1m: Difference between revisions

Revision as of 21:47, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3c1m.png

Template:STRUCTURE 3c1m

Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartateCyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate

Template:ABSTRACT PUBMED 18334478

About this StructureAbout this Structure

3C1M is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

ReferenceReference

The structural basis for allosteric Inhibition of a threonine-sensitive aspartokinase., Liu X, Pavlovsky AG, Viola RE, J Biol Chem. 2008 Mar 11;. PMID:18334478

Page seeded by OCA on Mon Jul 28 21:47:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3c1m.jpg|left|200px]]
+{{Seed}}
+[[Image:3c1m.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3c1m|  PDB=3c1m  |  SCENE=  }}
-'''Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate'''
+===Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate===
-==Overview==
+<!--
-The commitment step to the aspartate pathway of amino acid biosynthesis is the phosphorylation of aspartic acid catalyzed by aspartokinase (AK). Most microorganisms and plants have multiple forms of this enzyme, and many of these isofunctional enzymes are subject to feedback regulation by the end products of the pathway. However, the archeal species M. jannaschii has only a single, monofunctional form of AK. The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK (Angeles et al., Biochemistry 31, 799, 1992). Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. In contrast, the highly cooperative binding of the allosteric regulator L-threonine to multiple sites on this dimer of dimers leads to a more open enzyme structure. A comparison of these structures supports a mechanism for allosteric regulation of AK in which the domain movements induced by threonine binding causes displacement of the substrates from the enzyme resulting in a relaxed, inactive conformation.
+The line below this paragraph, {{ABSTRACT_PUBMED_18334478}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18334478 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18334478}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Threonine-sensitive]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 21:17:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:47:42 2008''