2hmf: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2hmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hmf, resolution 2.700Å" /> '''Structure of a Thre...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2hmf.gif|left|200px]]<br /><applet load="2hmf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2hmf.gif|left|200px]]<br /><applet load="2hmf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2hmf, resolution 2.700&Aring;" />
caption="2hmf, resolution 2.700&Aring;" />
'''Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate'''<br />
'''Structure of a Threonine Sensitive Aspartokinase from Methanococcus jannaschii Complexed with Mg-ADP and Aspartate'''<br />


==Overview==
==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.
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==
==About this Structure==
2HMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with MG, ADP and ASP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HMF OCA].  
2HMF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HMF OCA].  


==Reference==
==Reference==
The initial step in the archaeal aspartate biosynthetic pathway catalyzed by a monofunctional aspartokinase., Faehnle CR, Liu X, Pavlovsky A, Viola RE, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):962-6. Epub 2006 Sep 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17012784 17012784]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17012784 17012784]
[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Faehnle, C.R.]]
[[Category: Faehnle, C R.]]
[[Category: Viola, R.E.]]
[[Category: Viola, R E.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: ASP]]
[[Category: ASP]]
Line 21: Line 21:
[[Category: aspartokinase]]
[[Category: aspartokinase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:50:41 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:26 2008''