2erc
From Proteopedia
(New page: 200px<br /><applet load="2erc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2erc, resolution 3.03Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2erc.jpg|left|200px]]<br /><applet load="2erc" size=" | + | [[Image:2erc.jpg|left|200px]]<br /><applet load="2erc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2erc, resolution 3.03Å" /> | caption="2erc, resolution 3.03Å" /> | ||
'''CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE'''<br /> | '''CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The prevalent mechanism of bacterial resistance to erythromycin and other | + | The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (a naturally occurring variant of ErmC) from Bacillus subtilis has been determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM), followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain is well-conserved between the DNA, RNA, and small-molecule MTases. However, the C-terminal nucleic acid binding domain differs from the DNA-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases. |
==About this Structure== | ==About this Structure== | ||
| - | 2ERC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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:// | + | 2ERC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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=2ERC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rRNA (adenine-N(6)-)-methyltransferase]] | [[Category: rRNA (adenine-N(6)-)-methyltransferase]] | ||
[[Category: Abad-Zapatero, C.]] | [[Category: Abad-Zapatero, C.]] | ||
| - | [[Category: Bussiere, D | + | [[Category: Bussiere, D E.]] |
| - | [[Category: Dealwis, C | + | [[Category: Dealwis, C G.]] |
| - | [[Category: Muchmore, S | + | [[Category: Muchmore, S W.]] |
[[Category: Schluckebier, G.]] | [[Category: Schluckebier, G.]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
| Line 24: | Line 24: | ||
[[Category: rrna methyltransferase]] | [[Category: rrna methyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:13:48 2008'' |
Revision as of 15:13, 21 February 2008
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CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE
Overview
The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (a naturally occurring variant of ErmC) from Bacillus subtilis has been determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM), followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain is well-conserved between the DNA, RNA, and small-molecule MTases. However, the C-terminal nucleic acid binding domain differs from the DNA-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases.
About this Structure
2ERC is a Single protein structure of sequence from Bacillus subtilis. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria., Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C, Biochemistry. 1998 May 19;37(20):7103-12. PMID:9585521
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