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2hmf

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[[Image:2hmf.gif|left|200px]]
[[Image:2hmf.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2hmf |SIZE=350|CAPTION= <scene name='initialview01'>2hmf</scene>, resolution 2.700&Aring;
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The line below this paragraph, containing "STRUCTURE_2hmf", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2hmf| PDB=2hmf | SCENE= }}
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|RELATEDENTRY=[[2cdq|2CDQ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hmf OCA], [http://www.ebi.ac.uk/pdbsum/2hmf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hmf RCSB]</span>
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}}
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'''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'''
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[[Category: Faehnle, C R.]]
[[Category: Faehnle, C R.]]
[[Category: Viola, R E.]]
[[Category: Viola, R E.]]
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[[Category: aspartokinase]]
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[[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 Mar 31 03:32:18 2008''
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Revision as of 03:27, 4 May 2008

Image:2hmf.gif

Template:STRUCTURE 2hmf

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


Overview

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.

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 Page seeded by OCA on Sun May 4 06:27:30 2008

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