2hmf

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[[Image:2hmf.gif|left|200px]]
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{{STRUCTURE_2hmf| PDB=2hmf | SCENE= }}
{{STRUCTURE_2hmf| PDB=2hmf | SCENE= }}
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'''Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate'''
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===Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate===
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==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.
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(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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:27:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:56:47 2008''

Revision as of 23:56, 27 July 2008

Template:STRUCTURE 2hmf

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

Template:ABSTRACT PUBMED 17012784

About this Structure

2HMF is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase., Faehnle CR, Liu X, Pavlovsky A, Viola RE, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):962-6. Epub 2006 Sep 30. PMID:17012784

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