1x7p: Difference between revisions

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[[Image:1x7p.gif|left|200px]]<br /><applet load="1x7p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1x7p.gif|left|200px]]<br /><applet load="1x7p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1x7p, resolution 2.55Å" />

'''Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes in complex with the cofactor AdoMet'''<br />

==Overview==

The emergence of antibiotic-resistant bacterial strains is a widespread, problem in medical practice and drug design, and each case requires the, elucidation of the underlying mechanism. AviRb from Streptomyces, viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal, RNA in Gram-positive bacteria and thus mediates resistance to the, oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of, AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was, determined, showing that it is a homodimer belonging to the SpoU family, within the SPOUT class of methyltransferases. The relationships within, this class were analyzed in detail and, in addition, a novel fourth SpoU, sequence fingerprint is proposed. Each subunit of AviRb consists of two, domains. The N-terminal domain, being related to the ribosomal proteins, L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to, all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot, of the polypeptide in an unusually bent conformation. The transferred, methyl group points to a broad cleft formed with the L30-type domain of, the other subunit. Measurements of mutant activity revealed four important, residues responsible for catalysis and allowed the modeling of a complex, between AviRb and the RNA target. The model includes a specificity pocket, for uracil but does not contain a base for deprotonating the 2'-O atom of, U2479 on methylation.

The emergence of antibiotic-resistant bacterial strains is a widespread problem in medical practice and drug design, and each case requires the elucidation of the underlying mechanism. AviRb from Streptomyces viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal RNA in Gram-positive bacteria and thus mediates resistance to the oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was determined, showing that it is a homodimer belonging to the SpoU family within the SPOUT class of methyltransferases. The relationships within this class were analyzed in detail and, in addition, a novel fourth SpoU sequence fingerprint is proposed. Each subunit of AviRb consists of two domains. The N-terminal domain, being related to the ribosomal proteins L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot of the polypeptide in an unusually bent conformation. The transferred methyl group points to a broad cleft formed with the L30-type domain of the other subunit. Measurements of mutant activity revealed four important residues responsible for catalysis and allowed the modeling of a complex between AviRb and the RNA target. The model includes a specificity pocket for uracil but does not contain a base for deprotonating the 2'-O atom of U2479 on methylation.

==About this Structure==

1X7P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes] 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=1X7P OCA].

1X7P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes] 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=1X7P OCA].

==Reference==

Line 14:

[[Category: Streptomyces viridochromogenes]]

[[Category: Bechthold, A.]]

[[Category: Mosbacher, T.G.]]

[[Category: Mosbacher, T G.]]

[[Category: Schulz, G.E.]]

[[Category: Schulz, G E.]]

[[Category: SAM]]

[[Category: bound cofactor adomet]]

Line 21:

[[Category: spou]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:51:51 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1x7p.gif|left|200px]]<br /><applet load="1x7p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1x7p.gif|left|200px]]<br /><applet load="1x7p" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1x7p, resolution 2.55&Aring;" />
 '''Crystal structure of the SpoU Methyltransferase AviRb from Streptomyces viridochromogenes in complex with the cofactor AdoMet'''<br />
 ==Overview==
-The emergence of antibiotic-resistant bacterial strains is a widespread, problem in medical practice and drug design, and each case requires the, elucidation of the underlying mechanism. AviRb from Streptomyces, viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal, RNA in Gram-positive bacteria and thus mediates resistance to the, oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of, AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was, determined, showing that it is a homodimer belonging to the SpoU family, within the SPOUT class of methyltransferases. The relationships within, this class were analyzed in detail and, in addition, a novel fourth SpoU, sequence fingerprint is proposed. Each subunit of AviRb consists of two, domains. The N-terminal domain, being related to the ribosomal proteins, L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to, all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot, of the polypeptide in an unusually bent conformation. The transferred, methyl group points to a broad cleft formed with the L30-type domain of, the other subunit. Measurements of mutant activity revealed four important, residues responsible for catalysis and allowed the modeling of a complex, between AviRb and the RNA target. The model includes a specificity pocket, for uracil but does not contain a base for deprotonating the 2'-O atom of, U2479 on methylation.
+The emergence of antibiotic-resistant bacterial strains is a widespread problem in medical practice and drug design, and each case requires the elucidation of the underlying mechanism. AviRb from Streptomyces viridochromogenes methylates the 2'-O atom of U2479 of the 23S ribosomal RNA in Gram-positive bacteria and thus mediates resistance to the oligosaccharide (orthosomycin) antibiotic avilamycin. The structure of AviRb with and without bound cofactor S-adenosyl-L-methionine (AdoMet) was determined, showing that it is a homodimer belonging to the SpoU family within the SPOUT class of methyltransferases. The relationships within this class were analyzed in detail and, in addition, a novel fourth SpoU sequence fingerprint is proposed. Each subunit of AviRb consists of two domains. The N-terminal domain, being related to the ribosomal proteins L30 and L7Ae, is likely to bind RNA. The C-terminal domain is related to all SPOUT methyltransferases, and is responsible for AdoMet-binding, catalysis and dimerization. The cofactor binds at the characteristic knot of the polypeptide in an unusually bent conformation. The transferred methyl group points to a broad cleft formed with the L30-type domain of the other subunit. Measurements of mutant activity revealed four important residues responsible for catalysis and allowed the modeling of a complex between AviRb and the RNA target. The model includes a specificity pocket for uracil but does not contain a base for deprotonating the 2'-O atom of U2479 on methylation.
 ==About this Structure==
-X7P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes] 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=1X7P OCA].
+X7P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_viridochromogenes Streptomyces viridochromogenes] 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=1X7P OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Streptomyces viridochromogenes]]
 [[Category: Bechthold, A.]]
-[[Category: Mosbacher, T.G.]]
+[[Category: Mosbacher, T G.]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: SAM]]
 [[Category: bound cofactor adomet]]
@@ Line 21: / Line 21: @@
 [[Category: spou]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:35:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:51:51 2008''