1yub

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(New page: 200px<br /><applet load="1yub" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yub" /> '''SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFER...)
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'''SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
'''SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
==Overview==
==Overview==
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The Erm family of methyltransferases is responsible for the development of, resistance to the macrolide-lincosamide-streptogramin type B (MLS), antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that, prevents the MLS antibiotics from binding to the ribosome and exhibiting, their antibacterial activity. Here we describe the three-dimensional, structure of an Erm family member, ErmAM, as determined by NMR, spectroscopy. The catalytic domain of ErmAM is structurally similar to, that found in other methyltransferases and consists of a seven-stranded, beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet., In contrast to the catalytic domain, the substrate binding domain is, different from other methyltransferases and adopts a novel fold that, consists of four alpha-helices.
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The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.
==About this Structure==
==About this Structure==
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1YUB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Active as [http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YUB OCA].
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1YUB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Active as [http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUB OCA].
==Reference==
==Reference==
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[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
[[Category: rRNA (adenine-N(6)-)-methyltransferase]]
[[Category: rRNA (adenine-N(6)-)-methyltransferase]]
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[[Category: Fesik, S.W.]]
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[[Category: Fesik, S W.]]
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[[Category: Holzman, T.F.]]
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[[Category: Holzman, T F.]]
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[[Category: Petros, A.M.]]
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[[Category: Petros, A M.]]
[[Category: Schnuchel, A.]]
[[Category: Schnuchel, A.]]
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[[Category: Severin, J.M.]]
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[[Category: Severin, J M.]]
[[Category: Walter, K.]]
[[Category: Walter, K.]]
[[Category: Yu, L.]]
[[Category: Yu, L.]]
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[[Category: rrna]]
[[Category: rrna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:09 2008''

Revision as of 14:09, 21 February 2008


1yub

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SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE

Overview

The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.

About this Structure

1YUB is a Single protein structure of sequence from Streptococcus pneumoniae. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 Full crystallographic information is available from OCA.

Reference

Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance., Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW, Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:9187657

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