1qs0

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(New page: 200px<br /><applet load="1qs0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qs0, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1qs0.jpg|left|200px]]<br /><applet load="1qs0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qs0, resolution 2.40&Aring;" />
caption="1qs0, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B)'''<br />
'''CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B)'''<br />
==Overview==
==Overview==
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The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of, the largest and most sophisticated protein assemblies known, with, molecular masses between 4 and 10 million Da. The principal enzyme, components, E1, E2 and E3, are present in numerous copies and utilize, multiple cofactors to catalyze a directed sequence of reactions via, substrate channeling. The crystal structure of a heterotetrameric, (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the, beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer., A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine, arm, leads to the active site, which contains the cofactor thiamin, diphosphate (ThDP) and an inhibitor-derived covalent modification of a, histidine side chain. The E1 structure, together with previous structural, information on E2 and E3, completes the picture of the shared, architectural features of these enormous macromolecular assemblies.
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The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. The principal enzyme components, E1, E2 and E3, are present in numerous copies and utilize multiple cofactors to catalyze a directed sequence of reactions via substrate channeling. The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine arm, leads to the active site, which contains the cofactor thiamin diphosphate (ThDP) and an inhibitor-derived covalent modification of a histidine side chain. The E1 structure, together with previous structural information on E2 and E3, completes the picture of the shared architectural features of these enormous macromolecular assemblies.
==About this Structure==
==About this Structure==
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1QS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with MG, COI and TDP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QS0 OCA].
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1QS0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=COI:'>COI</scene> and <scene name='pdbligand=TDP:'>TDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QS0 OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Aevarsson, A.]]
[[Category: Aevarsson, A.]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hol, W G.J.]]
[[Category: Seger, K.]]
[[Category: Seger, K.]]
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[[Category: Sokatch, J.R.]]
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[[Category: Sokatch, J R.]]
[[Category: Turley, S.]]
[[Category: Turley, S.]]
[[Category: COI]]
[[Category: COI]]
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[[Category: thdp cofactor]]
[[Category: thdp cofactor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:56:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:05 2008''

Revision as of 12:43, 21 February 2008


1qs0, resolution 2.40Å

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CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA 2-OXOISOVALERATE DEHYDROGENASE (BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE, E1B)

Overview

The family of giant multienzyme complexes metabolizing pyruvate, 2-oxoglutarate, branched-chain 2-oxo acids or acetoin contains several of the largest and most sophisticated protein assemblies known, with molecular masses between 4 and 10 million Da. The principal enzyme components, E1, E2 and E3, are present in numerous copies and utilize multiple cofactors to catalyze a directed sequence of reactions via substrate channeling. The crystal structure of a heterotetrameric (alpha2beta2) E1, 2-oxoisovalerate dehydrogenase from Pseudomonas putida, reveals a tightly packed arrangement of the four subunits with the beta2-dimer held between the jaws of a 'vise' formed by the alpha2-dimer. A long hydrophobic channel, suitable to accommodate the E2 lipoyl-lysine arm, leads to the active site, which contains the cofactor thiamin diphosphate (ThDP) and an inhibitor-derived covalent modification of a histidine side chain. The E1 structure, together with previous structural information on E2 and E3, completes the picture of the shared architectural features of these enormous macromolecular assemblies.

About this Structure

1QS0 is a Protein complex structure of sequences from Pseudomonas putida with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes., Aevarsson A, Seger K, Turley S, Sokatch JR, Hol WG, Nat Struct Biol. 1999 Aug;6(8):785-92. PMID:10426958

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