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1e3t

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(New page: 200px<br /><applet load="1e3t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e3t" /> '''SOLUTION STRUCTURE OF THE NADP(H) BINDING CO...)
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'''SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM'''<br />
'''SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM'''<br />
==Overview==
==Overview==
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Transhydrogenase is a proton pump found in the membranes of bacteria and, animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum, rubrum has been solved by NMR methods. This is the first description of, the structure of dIII from a bacterial source. The protein adopts a, Rossmann fold: an open, twisted, parallel beta-sheet, flanked by helices., However, the binding of NADP(+) to dIII is profoundly different to that, seen in other Rossmann structures, in that its orientation is reversed:, the adenosine moiety interacts with the first betaalphabetaalphabeta, motif, and the nicotinamide with the second. Features in the structure, that might be responsible for changes in nucleotide-binding affinity, during catalysis, and for interaction with other components of the enzyme, are identified. The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also, show the reversed nucleotide orientation.
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Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods. This is the first description of the structure of dIII from a bacterial source. The protein adopts a Rossmann fold: an open, twisted, parallel beta-sheet, flanked by helices. However, the binding of NADP(+) to dIII is profoundly different to that seen in other Rossmann structures, in that its orientation is reversed: the adenosine moiety interacts with the first betaalphabetaalphabeta motif, and the nicotinamide with the second. Features in the structure that might be responsible for changes in nucleotide-binding affinity during catalysis, and for interaction with other components of the enzyme, are identified. The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also show the reversed nucleotide orientation.
==About this Structure==
==About this Structure==
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1E3T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with NAP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E3T OCA].
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1E3T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] 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=1E3T OCA].
==Reference==
==Reference==
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[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cotton, N.P.J.]]
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[[Category: Cotton, N P.J.]]
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[[Category: Jackson, J.B.]]
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[[Category: Jackson, J B.]]
[[Category: Jeeves, M.]]
[[Category: Jeeves, M.]]
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[[Category: Quirk, P.G.]]
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[[Category: Quirk, P G.]]
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[[Category: Smith, K.J.]]
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[[Category: Smith, K J.]]
[[Category: NAP]]
[[Category: NAP]]
[[Category: membrane protein]]
[[Category: membrane protein]]
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[[Category: transhydrogenase]]
[[Category: transhydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:45:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:28 2008''

Revision as of 10:23, 21 February 2008


1e3t

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SOLUTION STRUCTURE OF THE NADP(H) BINDING COMPONENT (DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM RUBRUM

Overview

Transhydrogenase is a proton pump found in the membranes of bacteria and animal mitochondria. The solution structure of the expressed, 21.5 kDa, NADP(H)-binding component (dIII) of transhydrogenase from Rhodospirillum rubrum has been solved by NMR methods. This is the first description of the structure of dIII from a bacterial source. The protein adopts a Rossmann fold: an open, twisted, parallel beta-sheet, flanked by helices. However, the binding of NADP(+) to dIII is profoundly different to that seen in other Rossmann structures, in that its orientation is reversed: the adenosine moiety interacts with the first betaalphabetaalphabeta motif, and the nicotinamide with the second. Features in the structure that might be responsible for changes in nucleotide-binding affinity during catalysis, and for interaction with other components of the enzyme, are identified. The results are compared with the recently determined, high-resolution crystal structures of human and bovine dIII which also show the reversed nucleotide orientation.

About this Structure

1E3T is a Single protein structure of sequence from Rhodospirillum rubrum with as ligand. Active as NAD(P)(+) transhydrogenase (B-specific), with EC number 1.6.1.1 Full crystallographic information is available from OCA.

Reference

Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum., Jeeves M, Smith KJ, Quirk PG, Cotton NP, Jackson JB, Biochim Biophys Acta. 2000 Aug 15;1459(2-3):248-57. PMID:11004437

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