1i9g

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(New page: 200px<br /><applet load="1i9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9g, resolution 1.98&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1i9g.gif|left|200px]]<br /><applet load="1i9g" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1i9g.gif|left|200px]]<br /><applet load="1i9g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i9g, resolution 1.98&Aring;" />
caption="1i9g, resolution 1.98&Aring;" />
'''CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE'''<br />
'''CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE'''<br />
==Overview==
==Overview==
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Rv2118c belongs to the class of conserved hypothetical proteins from, Mycobacterium tuberculosis H37Rv. The crystal structure of Rv2118c in, complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98, A resolution. The crystallographic asymmetric unit consists of a monomer, but symmetry-related subunits interact extensively, leading to a, tetrameric structure. The structure of the monomer can be divided, functionally into two domains: the larger catalytic C-terminal domain that, binds the cofactor AdoMet and is involved in the transfer of methyl group, from AdoMet to the substrate and a smaller N-terminal domain. The, structure of the catalytic domain is very similar to that of other, AdoMet-dependent methyltransferases. The N-terminal domain is primarily a, beta-structure with a fold not found in other methyltransferases of known, structure. Database searches reveal a conserved family of Rv2118c-like, proteins from various organisms. Multiple sequence alignments show several, regions of high sequence similarity (motifs) in this family of proteins., Structure analysis and homology to yeast Gcd14p suggest that Rv2118c could, be an RNA methyltransferase, but further studies are required to establish, its functional role conclusively. Copyright 12001 Academic Press.
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Rv2118c belongs to the class of conserved hypothetical proteins from Mycobacterium tuberculosis H37Rv. The crystal structure of Rv2118c in complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98 A resolution. The crystallographic asymmetric unit consists of a monomer, but symmetry-related subunits interact extensively, leading to a tetrameric structure. The structure of the monomer can be divided functionally into two domains: the larger catalytic C-terminal domain that binds the cofactor AdoMet and is involved in the transfer of methyl group from AdoMet to the substrate and a smaller N-terminal domain. The structure of the catalytic domain is very similar to that of other AdoMet-dependent methyltransferases. The N-terminal domain is primarily a beta-structure with a fold not found in other methyltransferases of known structure. Database searches reveal a conserved family of Rv2118c-like proteins from various organisms. Multiple sequence alignments show several regions of high sequence similarity (motifs) in this family of proteins. Structure analysis and homology to yeast Gcd14p suggest that Rv2118c could be an RNA methyltransferase, but further studies are required to establish its functional role conclusively. Copyright 12001 Academic Press.
==About this Structure==
==About this Structure==
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1I9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I9G OCA].
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1I9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9G OCA].
==Reference==
==Reference==
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[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dineshkumar, T.K.]]
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[[Category: Dineshkumar, T K.]]
[[Category: Gupta, A.]]
[[Category: Gupta, A.]]
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[[Category: Kumar, P.H.]]
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[[Category: Kumar, P H.]]
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[[Category: Subramanya, H.S.]]
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[[Category: Subramanya, H S.]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: TBSGC, TB Structural Genomics Consortium.]]
[[Category: Varshney, U.]]
[[Category: Varshney, U.]]
[[Category: SAM]]
[[Category: SAM]]
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[[Category: tbsgc]]
[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:48:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:27 2008''

Revision as of 11:09, 21 February 2008


1i9g, resolution 1.98Å

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CRYSTAL STRUCTURE OF AN ADOMET DEPENDENT METHYLTRANSFERASE

Overview

Rv2118c belongs to the class of conserved hypothetical proteins from Mycobacterium tuberculosis H37Rv. The crystal structure of Rv2118c in complex with S-adenosyl-l-methionine (AdoMet) has been determined at 1.98 A resolution. The crystallographic asymmetric unit consists of a monomer, but symmetry-related subunits interact extensively, leading to a tetrameric structure. The structure of the monomer can be divided functionally into two domains: the larger catalytic C-terminal domain that binds the cofactor AdoMet and is involved in the transfer of methyl group from AdoMet to the substrate and a smaller N-terminal domain. The structure of the catalytic domain is very similar to that of other AdoMet-dependent methyltransferases. The N-terminal domain is primarily a beta-structure with a fold not found in other methyltransferases of known structure. Database searches reveal a conserved family of Rv2118c-like proteins from various organisms. Multiple sequence alignments show several regions of high sequence similarity (motifs) in this family of proteins. Structure analysis and homology to yeast Gcd14p suggest that Rv2118c could be an RNA methyltransferase, but further studies are required to establish its functional role conclusively. Copyright 12001 Academic Press.

About this Structure

1I9G is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of Rv2118c: an AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv., Gupta A, Kumar PH, Dineshkumar TK, Varshney U, Subramanya HS, J Mol Biol. 2001 Sep 14;312(2):381-91. PMID:11554794

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