2bud

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(New page: 200px<br /><applet load="2bud" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bud" /> '''THE SOLUTION STRUCTURE OF THE CHROMO BARREL ...)
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'''THE SOLUTION STRUCTURE OF THE CHROMO BARREL DOMAIN FROM THE MALES-ABSENT ON THE FIRST (MOF) PROTEIN'''<br />
'''THE SOLUTION STRUCTURE OF THE CHROMO BARREL DOMAIN FROM THE MALES-ABSENT ON THE FIRST (MOF) PROTEIN'''<br />
==Overview==
==Overview==
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We report here the structure of the putative chromo domain from MOF, a, member of the MYST family of histone acetyltransferases that acetylates, histone H4 at Lys-16 and is part of the dosage compensation complex in, Drosophila. We found that the structure of this domain is a beta-barrel, that is distinct from the alpha + beta fold of the canonical chromo, domain. Despite the differences, there are similarities that support an, evolutionary relationship between the two domains, and we propose the name, "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved, aromatic residues is present or not. The structure suggests that, although, the MOF-like domains may have a role in RNA binding, the MSL3-like domains, could instead bind methylated residues. The MOF chromo barrel shares a, common fold with other chromatin-associated modules, including the, MBT-like repeat, Tudor, and PWWP domains. This structural similarity, suggests a probable evolutionary pathway from these other modules to the, canonical chromo domains (or vice versa) with the chromo barrel domain, representing an intermediate structure.
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We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.
==About this Structure==
==About this Structure==
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2BUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BUD OCA].
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2BUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Histone_acetyltransferase Histone acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.48 2.3.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUD OCA].
==Reference==
==Reference==
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[[Category: Akhtar, A.]]
[[Category: Akhtar, A.]]
[[Category: Buscaino, A.]]
[[Category: Buscaino, A.]]
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[[Category: Laue, E.D.]]
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[[Category: Laue, E D.]]
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[[Category: Murzin, A.G.]]
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[[Category: Murzin, A G.]]
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[[Category: Murzina, N.V.]]
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[[Category: Murzina, N V.]]
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[[Category: Nielsen, P.R.]]
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[[Category: Nielsen, P R.]]
[[Category: Nietlispach, D.]]
[[Category: Nietlispach, D.]]
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[[Category: Warner, R.J.]]
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[[Category: Warner, R J.]]
[[Category: acetyl-transfer]]
[[Category: acetyl-transfer]]
[[Category: beta barrel]]
[[Category: beta barrel]]
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[[Category: transferase acyltransferase]]
[[Category: transferase acyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:55:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:49 2008''

Revision as of 14:41, 21 February 2008


2bud

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THE SOLUTION STRUCTURE OF THE CHROMO BARREL DOMAIN FROM THE MALES-ABSENT ON THE FIRST (MOF) PROTEIN

Overview

We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.

About this Structure

2BUD is a Single protein structure of sequence from Drosophila melanogaster. Active as Histone acetyltransferase, with EC number 2.3.1.48 Full crystallographic information is available from OCA.

Reference

Structure of the chromo barrel domain from the MOF acetyltransferase., Nielsen PR, Nietlispach D, Buscaino A, Warner RJ, Akhtar A, Murzin AG, Murzina NV, Laue ED, J Biol Chem. 2005 Sep 16;280(37):32326-31. Epub 2005 Jun 17. PMID:15964847

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