1ni4

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[[Image:1ni4.gif|left|200px]]<br /><applet load="1ni4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ni4.gif|left|200px]]
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caption="1ni4, resolution 1.95&Aring;" />
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'''HUMAN PYRUVATE DEHYDROGENASE'''<br />
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{{Structure
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|PDB= 1ni4 |SIZE=350|CAPTION= <scene name='initialview01'>1ni4</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=TPP:THIAMINE DIPHOSPHATE'>TPP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1]
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|GENE=
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}}
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'''HUMAN PYRUVATE DEHYDROGENASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NI4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=TPP:'>TPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pyruvate_dehydrogenase_(acetyl-transferring) Pyruvate dehydrogenase (acetyl-transferring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.4.1 1.2.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NI4 OCA].
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1NI4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NI4 OCA].
==Reference==
==Reference==
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Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase., Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS, J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12651851 12651851]
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Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase., Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS, J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12651851 12651851]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: thiamin pyrophosphate]]
[[Category: thiamin pyrophosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:10 2008''

Revision as of 10:57, 20 March 2008


PDB ID 1ni4

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , and
Activity: Pyruvate dehydrogenase (acetyl-transferring), with EC number 1.2.4.1
Coordinates: save as pdb, mmCIF, xml



HUMAN PYRUVATE DEHYDROGENASE


Contents

Overview

The derivative of vitamin B1, thiamin pyrophosphate, is a cofactor of enzymes performing catalysis in pathways of energy production. In alpha2beta2-heterotetrameric human pyruvate dehydrogenase, this cofactor is used to cleave the Calpha-C(=O) bond of pyruvate followed by reductive acetyl transfer to lipoyl-dihydrolipoamide acetyltransferase. The dynamic nonequivalence of two, otherwise chemically equivalent, catalytic sites has not yet been understood. To understand the mechanism of action of this enzyme, we determined the crystal structure of the holo-form of human pyruvate dehydrogenase at 1.95-A resolution. We propose a model for the flip-flop action of this enzyme through a concerted approximately 2-A shuttle-like motion of its heterodimers. Similarity of thiamin pyrophosphate binding in human pyruvate dehydrogenase with functionally related enzymes suggests that this newly defined shuttle-like motion of domains is common to the family of thiamin pyrophosphate-dependent enzymes.

Disease

Known diseases associated with this structure: Leigh syndrome, X-linked OMIM:[300502], Pyruvate dehydrogenase E1-beta deficiency OMIM:[179060], Pyruvate dehydrogenase deficiency OMIM:[300502]

About this Structure

1NI4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase., Ciszak EM, Korotchkina LG, Dominiak PM, Sidhu S, Patel MS, J Biol Chem. 2003 Jun 6;278(23):21240-6. Epub 2003 Mar 21. PMID:12651851

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