This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hmf
From Proteopedia
(New page: 200px<br /><applet load="2hmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hmf, resolution 2.700Å" /> '''Structure of a Thre...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2hmf.gif|left|200px]]<br /><applet load="2hmf" size=" | + | [[Image:2hmf.gif|left|200px]]<br /><applet load="2hmf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hmf, resolution 2.700Å" /> | caption="2hmf, resolution 2.700Å" /> | ||
'''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 | + | 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:// | + | 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 | + | 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 | + | [[Category: Faehnle, C R.]] |
| - | [[Category: Viola, R | + | [[Category: Viola, R E.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: ASP]] | [[Category: ASP]] | ||
| Line 21: | Line 21: | ||
[[Category: aspartokinase]] | [[Category: aspartokinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:43:26 2008'' |
Revision as of 15:43, 21 February 2008
|
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 with , and as ligands. Active as Aspartate kinase, with EC number 2.7.2.4 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 Thu Feb 21 17:43:26 2008
