1d4o

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[[Image:1d4o.jpg|left|200px]]<br /><applet load="1d4o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1d4o.jpg|left|200px]]
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caption="1d4o, resolution 1.21&Aring;" />
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'''CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 1d4o |SIZE=350|CAPTION= <scene name='initialview01'>1d4o</scene>, resolution 1.21&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAP:NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NAP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(B-specific) NAD(P)(+) transhydrogenase (B-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.1 1.6.1.1]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1D4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(B-specific) NAD(P)(+) transhydrogenase (B-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.1 1.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4O OCA].
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1D4O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4O OCA].
==Reference==
==Reference==
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Crystal structure of transhydrogenase domain III at 1.2 A resolution., Prasad GS, Sridhar V, Yamaguchi M, Hatefi Y, Stout CD, Nat Struct Biol. 1999 Dec;6(12):1126-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10581554 10581554]
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Crystal structure of transhydrogenase domain III at 1.2 A resolution., Prasad GS, Sridhar V, Yamaguchi M, Hatefi Y, Stout CD, Nat Struct Biol. 1999 Dec;6(12):1126-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581554 10581554]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: NAD(P)(+) transhydrogenase (B-specific)]]
[[Category: NAD(P)(+) transhydrogenase (B-specific)]]
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[[Category: protein-nadp(h) complex]]
[[Category: protein-nadp(h) complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:32:48 2008''

Revision as of 08:32, 20 March 2008


PDB ID 1d4o

Drag the structure with the mouse to rotate
, resolution 1.21Å
Ligands:
Activity: NAD(P)(+) transhydrogenase (B-specific), with EC number 1.6.1.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF TRANSHYDROGENASE DOMAIN III AT 1.2 ANGSTROMS RESOLUTION


Overview

The nicotinamide nucleotide transhydrogenases (TH) of mitochondria and bacteria are membrane-intercalated proton pumps that transduce substrate binding energy and protonmotive force via protein conformational changes. In mitochondria, TH utilizes protonmotive force to promote direct hydride ion transfer from NADH to NADP, which are bound at the distinct extramembranous domains I and III, respectively. Domain II is the membrane-intercalated domain and contains the enzyme's proton channel. This paper describes the crystal structure of the NADP(H) binding domain III of bovine TH at 1.2 A resolution. The structure reveals that NADP is bound in a manner inverted from that previously observed for nucleotide binding folds. The non-classical binding mode exposes the NADP(H) nicotinamide ring for direct contact with NAD(H) in domain I, in accord with biochemical data. The surface of domain III surrounding the exposed nicotinamide is comprised of conserved residues presumed to form the interface with domain I during hydride ion transfer. Further, an adjacent region contains a number of acidic residues, forming a surface with negative electrostatic potential which may interact with extramembranous loops of domain II. Together, the distinctive surface features allow mechanistic considerations regarding the NADP(H)-promoted conformation changes that are involved in the interactions of domain III with domains I and II for hydride ion transfer and proton translocation.

About this Structure

1D4O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of transhydrogenase domain III at 1.2 A resolution., Prasad GS, Sridhar V, Yamaguchi M, Hatefi Y, Stout CD, Nat Struct Biol. 1999 Dec;6(12):1126-31. PMID:10581554

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