1jm6

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(New page: 200px<br /><applet load="1jm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jm6, resolution 2.50&Aring;" /> '''Pyruvate dehydrogena...)
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[[Image:1jm6.jpg|left|200px]]<br /><applet load="1jm6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jm6.jpg|left|200px]]<br /><applet load="1jm6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jm6, resolution 2.50&Aring;" />
caption="1jm6, resolution 2.50&Aring;" />
'''Pyruvate dehydrogenase kinase, isozyme 2, containing ADP'''<br />
'''Pyruvate dehydrogenase kinase, isozyme 2, containing ADP'''<br />
==Overview==
==Overview==
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The structure of mitochondrial pyruvate dehydrogenase kinase isozyme 2 is, of interest because it represents a family of serine-specific protein, kinases that lack sequence similarity with all other eukaryotic protein, kinases. Similarity exists instead with key motifs of prokaryotic, histidine protein kinases and a family of eukaryotic ATPases. The 2.5-A, crystal structure reported here reveals that pyruvate dehydrogenase kinase, isozyme 2 has two domains of about the same size. The N-terminal half is, dominated by a bundle of four amphipathic alpha-helices, whereas the, C-terminal half is folded into an alpha/beta sandwich that contains the, nucleotide-binding site. Analysis of the structure reveals this C-terminal, domain to be very similar to the nucleotide-binding domain of bacterial, histidine kinases, but the catalytic mechanism appears similar to that of, the eukaryotic serine kinases and ATPases.
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The structure of mitochondrial pyruvate dehydrogenase kinase isozyme 2 is of interest because it represents a family of serine-specific protein kinases that lack sequence similarity with all other eukaryotic protein kinases. Similarity exists instead with key motifs of prokaryotic histidine protein kinases and a family of eukaryotic ATPases. The 2.5-A crystal structure reported here reveals that pyruvate dehydrogenase kinase isozyme 2 has two domains of about the same size. The N-terminal half is dominated by a bundle of four amphipathic alpha-helices, whereas the C-terminal half is folded into an alpha/beta sandwich that contains the nucleotide-binding site. Analysis of the structure reveals this C-terminal domain to be very similar to the nucleotide-binding domain of bacterial histidine kinases, but the catalytic mechanism appears similar to that of the eukaryotic serine kinases and ATPases.
==About this Structure==
==About this Structure==
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1JM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Pyruvate_dehydrogenase_(acetyl-transferring)]_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.2 2.7.11.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JM6 OCA].
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1JM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Pyruvate_dehydrogenase_(acetyl-transferring)]_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.2 2.7.11.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JM6 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: [Pyruvate dehydrogenase (acetyl-transferring)] kinase]]
[[Category: [Pyruvate dehydrogenase (acetyl-transferring)] kinase]]
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[[Category: Bowker-Kinley, M.M.]]
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[[Category: Bowker-Kinley, M M.]]
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[[Category: Hamilton, J.A.]]
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[[Category: Hamilton, J A.]]
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[[Category: Harris, R.A.]]
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[[Category: Harris, R A.]]
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[[Category: Popov, K.M.]]
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[[Category: Popov, K M.]]
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[[Category: Sloan, R.B.]]
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[[Category: Sloan, R B.]]
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[[Category: Steussy, C.N.]]
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[[Category: Steussy, C N.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: serine kinase]]
[[Category: serine kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:22:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:11 2008''

Revision as of 11:24, 21 February 2008


1jm6, resolution 2.50Å

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Pyruvate dehydrogenase kinase, isozyme 2, containing ADP

Overview

The structure of mitochondrial pyruvate dehydrogenase kinase isozyme 2 is of interest because it represents a family of serine-specific protein kinases that lack sequence similarity with all other eukaryotic protein kinases. Similarity exists instead with key motifs of prokaryotic histidine protein kinases and a family of eukaryotic ATPases. The 2.5-A crystal structure reported here reveals that pyruvate dehydrogenase kinase isozyme 2 has two domains of about the same size. The N-terminal half is dominated by a bundle of four amphipathic alpha-helices, whereas the C-terminal half is folded into an alpha/beta sandwich that contains the nucleotide-binding site. Analysis of the structure reveals this C-terminal domain to be very similar to the nucleotide-binding domain of bacterial histidine kinases, but the catalytic mechanism appears similar to that of the eukaryotic serine kinases and ATPases.

About this Structure

1JM6 is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as [Pyruvate_dehydrogenase_(acetyl-transferring)_kinase [Pyruvate dehydrogenase (acetyl-transferring)] kinase], with EC number 2.7.11.2 Full crystallographic information is available from OCA.

Reference

Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase., Steussy CN, Popov KM, Bowker-Kinley MM, Sloan RB Jr, Harris RA, Hamilton JA, J Biol Chem. 2001 Oct 5;276(40):37443-50. Epub 2001 Aug 1. PMID:11483605[[Category: [Pyruvate dehydrogenase (acetyl-transferring)] kinase]]

Page seeded by OCA on Thu Feb 21 13:24:11 2008

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