2hmf: Difference between revisions

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[[Image:2hmf.gif|left|200px]]
{{Seed}}
[[Image:2hmf.png|left|200px]]


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{{STRUCTURE_2hmf|  PDB=2hmf  |  SCENE=  }}  
{{STRUCTURE_2hmf|  PDB=2hmf  |  SCENE=  }}  


'''Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate'''
===Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate===




==Overview==
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The activation of the beta-carboxyl group of aspartate catalyzed by aspartokinase is the commitment step to amino-acid biosynthesis in the aspartate pathway. The first structure of a microbial aspartokinase, that from Methanococcus jannaschii, has been determined in the presence of the amino-acid substrate L-aspartic acid and the nucleotide product MgADP. The enzyme assembles into a dimer of dimers, with the interfaces mediated by both the N- and C-terminal domains. The active-site functional groups responsible for substrate binding and specificity have been identified and roles have been proposed for putative catalytic functional groups.
The line below this paragraph, {{ABSTRACT_PUBMED_17012784}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17012784 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17012784}}


==About this Structure==
==About this Structure==
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[[Category: Viola, R E.]]
[[Category: Viola, R E.]]
[[Category: Aspartokinase]]
[[Category: Aspartokinase]]
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