1om2

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(New page: 200px<br /><applet load="1om2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1om2" /> '''SOLUTION NMR STRUCTURE OF THE MITOCHONDRIAL ...)
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'''SOLUTION NMR STRUCTURE OF THE MITOCHONDRIAL PROTEIN IMPORT RECEPTOR TOM20 FROM RAT IN A COMPLEX WITH A PRESEQUENCE PEPTIDE DERIVED FROM RAT ALDEHYDE DEHYDROGENASE (ALDH)'''<br />
'''SOLUTION NMR STRUCTURE OF THE MITOCHONDRIAL PROTEIN IMPORT RECEPTOR TOM20 FROM RAT IN A COMPLEX WITH A PRESEQUENCE PEPTIDE DERIVED FROM RAT ALDEHYDE DEHYDROGENASE (ALDH)'''<br />
==Overview==
==Overview==
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Most mitochondrial proteins are synthesized in the cytosol as precursor, proteins with a cleavable N-terminal presequence and are imported into, mitochondria. We report here the NMR structure of a general import, receptor, rat Tom20, in a complex with a presequence peptide derived from, rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all, alpha-helical structure with a groove to accommodate the presequence, peptide. The bound presequence forms an amphiphilic helical structure with, hydrophobic leucines aligned on one side to interact with a hydrophobic, patch in the Tom20 groove. Although the positive charges of the, presequence are essential for import ability, presequence binding to Tom20, is mediated mainly by hydrophobic rather than ionic interactions.
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Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all alpha-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.
==About this Structure==
==About this Structure==
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1OM2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(+)) Aldehyde dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.3 1.2.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OM2 OCA].
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1OM2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(+)) Aldehyde dehydrogenase (NAD(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.3 1.2.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OM2 OCA].
==Reference==
==Reference==
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[[Category: receptor for presequences]]
[[Category: receptor for presequences]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:00:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:12 2008''

Revision as of 12:19, 21 February 2008

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1om2

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SOLUTION NMR STRUCTURE OF THE MITOCHONDRIAL PROTEIN IMPORT RECEPTOR TOM20 FROM RAT IN A COMPLEX WITH A PRESEQUENCE PEPTIDE DERIVED FROM RAT ALDEHYDE DEHYDROGENASE (ALDH)

Overview

Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex with a presequence peptide derived from rat aldehyde dehydrogenase. The cytosolic domain of Tom20 forms an all alpha-helical structure with a groove to accommodate the presequence peptide. The bound presequence forms an amphiphilic helical structure with hydrophobic leucines aligned on one side to interact with a hydrophobic patch in the Tom20 groove. Although the positive charges of the presequence are essential for import ability, presequence binding to Tom20 is mediated mainly by hydrophobic rather than ionic interactions.

About this Structure

1OM2 is a Protein complex structure of sequences from Rattus norvegicus. Active as Aldehyde dehydrogenase (NAD(+)), with EC number 1.2.1.3 Full crystallographic information is available from OCA.

Reference

Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20., Abe Y, Shodai T, Muto T, Mihara K, Torii H, Nishikawa S, Endo T, Kohda D, Cell. 2000 Mar 3;100(5):551-60. PMID:10721992

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