1f6m

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[[Image:1f6m.gif|left|200px]]<br /><applet load="1f6m" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f6m.gif|left|200px]]
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caption="1f6m, resolution 2.95&Aring;" />
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'''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+'''<br />
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{{Structure
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|PDB= 1f6m |SIZE=350|CAPTION= <scene name='initialview01'>1f6m</scene>, resolution 2.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=3AA:3-AMINOPYRIDINE-ADENINE DINUCLEOTIDE PHOSPHATE'>3AA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1F6M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=3AA:'>3AA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6M OCA].
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1F6M is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6M OCA].
==Reference==
==Reference==
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Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase., Lennon BW, Williams CH Jr, Ludwig ML, Science. 2000 Aug 18;289(5482):1190-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10947986 10947986]
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Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase., Lennon BW, Williams CH Jr, Ludwig ML, Science. 2000 Aug 18;289(5482):1190-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10947986 10947986]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ternary complex]]
[[Category: ternary complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:08 2008''

Revision as of 09:05, 20 March 2008


PDB ID 1f6m

Drag the structure with the mouse to rotate
, resolution 2.95Å
Ligands: and
Activity: Thioredoxin-disulfide reductase, with EC number 1.8.1.9
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+


Overview

In thioredoxin reductase (TrxR) from Escherichia coli, cycles of reduction and reoxidation of the flavin adenine dinucleotide (FAD) cofactor depend on rate-limiting rearrangements of the FAD and NADPH (reduced form of nicotinamide adenine dinucleotide phosphate) domains. We describe the structure of the flavin-reducing conformation of E. coli TrxR at a resolution of 3.0 angstroms. The orientation of the two domains permits reduction of FAD by NADPH and oxidation of the enzyme dithiol by the protein substrate, thioredoxin. The alternate conformation, described by Kuriyan and co-workers, permits internal transfer of reducing equivalents from reduced FAD to the active-site disulfide. Comparison of these structures demonstrates that switching between the two conformations involves a "ball-and-socket" motion in which the pyridine nucleotide-binding domain rotates by 67 degrees.

About this Structure

1F6M is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase., Lennon BW, Williams CH Jr, Ludwig ML, Science. 2000 Aug 18;289(5482):1190-4. PMID:10947986

Page seeded by OCA on Thu Mar 20 11:05:08 2008

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