1uwv
From Proteopedia
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==Overview== | ==Overview== | ||
| - | RumA catalyzes transfer of a methyl group from S-adenosylmethionine (SAM) | + | RumA catalyzes transfer of a methyl group from S-adenosylmethionine (SAM) specifically to uridine 1939 of 23S ribosomal RNA in Escherichia coli to yield 5-methyluridine. We determined the crystal structure of RumA at 1.95 A resolution. The protein is organized into three structural domains: The N-terminal domain contains sequence homology to the conserved TRAM motif and displays a five-stranded beta barrel architecture characteristic of an oligosaccharide/oligonucleotide binding fold. The central domain contains a [Fe(4)S(4)] cluster coordinated by four conserved cysteine residues. The C-terminal domain displays the typical SAM-dependent methyltransferase fold. The catalytic nucleophile Cys389 lies in a motif different from that in DNA 5-methylcytosine methyltransferases. The electrostatic potential surface reveals a predominately positively charged area that covers the concave surface of the first two domains and suggests an RNA binding mode. The iron-sulfur cluster may be involved in the correct folding of the protein or may have a role in RNA binding. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Agarwalla, S.]] | [[Category: Agarwalla, S.]] | ||
| - | [[Category: Lee, T | + | [[Category: Lee, T T.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: NI]] | [[Category: NI]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:12 2008'' |
Revision as of 13:29, 21 February 2008
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CRYSTAL STRUCTURE OF RUMA, THE IRON-SULFUR CLUSTER CONTAINING E. COLI 23S RIBOSOMAL RNA 5-METHYLURIDINE METHYLTRANSFERASE
Overview
RumA catalyzes transfer of a methyl group from S-adenosylmethionine (SAM) specifically to uridine 1939 of 23S ribosomal RNA in Escherichia coli to yield 5-methyluridine. We determined the crystal structure of RumA at 1.95 A resolution. The protein is organized into three structural domains: The N-terminal domain contains sequence homology to the conserved TRAM motif and displays a five-stranded beta barrel architecture characteristic of an oligosaccharide/oligonucleotide binding fold. The central domain contains a [Fe(4)S(4)] cluster coordinated by four conserved cysteine residues. The C-terminal domain displays the typical SAM-dependent methyltransferase fold. The catalytic nucleophile Cys389 lies in a motif different from that in DNA 5-methylcytosine methyltransferases. The electrostatic potential surface reveals a predominately positively charged area that covers the concave surface of the first two domains and suggests an RNA binding mode. The iron-sulfur cluster may be involved in the correct folding of the protein or may have a role in RNA binding.
About this Structure
1UWV is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of RumA, an iron-sulfur cluster containing E. coli ribosomal RNA 5-methyluridine methyltransferase., Lee TT, Agarwalla S, Stroud RM, Structure. 2004 Mar;12(3):397-407. PMID:15016356
Page seeded by OCA on Thu Feb 21 15:29:12 2008
Categories: Escherichia coli | Single protein | Agarwalla, S. | Lee, T T. | Stroud, R M. | CL | NI | PO4 | SF4 | Iron-sulfur cluster | Methyltransferase | Rna modification | Rna processing | Transferase
