2nxn
From Proteopedia
(New page: 200px<br /><applet load="2nxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nxn, resolution 2.40Å" /> '''T. thermophilus ribo...) |
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| - | [[Image:2nxn.jpg|left|200px]]<br /><applet load="2nxn" size=" | + | [[Image:2nxn.jpg|left|200px]]<br /><applet load="2nxn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2nxn, resolution 2.40Å" /> | caption="2nxn, resolution 2.40Å" /> | ||
'''T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11'''<br /> | '''T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial ribosomal protein L11 is post-translationally trimethylated at | + | Bacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 A resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit. |
==About this Structure== | ==About this Structure== | ||
| - | 2NXN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http:// | + | 2NXN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
| - | [[Category: Dahlberg, A | + | [[Category: Dahlberg, A E.]] |
[[Category: Demirci, H.]] | [[Category: Demirci, H.]] | ||
| - | [[Category: Gregory, S | + | [[Category: Gregory, S T.]] |
[[Category: Jogl, G.]] | [[Category: Jogl, G.]] | ||
[[Category: post-translational modification]] | [[Category: post-translational modification]] | ||
[[Category: s-adenosyl-l-methionine dependent methyltransferase]] | [[Category: s-adenosyl-l-methionine dependent methyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:11 2008'' |
Revision as of 16:12, 21 February 2008
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T. thermophilus ribosomal protein L11 methyltransferase (PrmA) in complex with ribosomal protein L11
Overview
Bacterial ribosomal protein L11 is post-translationally trimethylated at multiple residues by a single methyltransferase, PrmA. Here, we describe four structures of PrmA from the extreme thermophile Thermus thermophilus. Two apo-PrmA structures at 1.59 and 2.3 A resolution and a third with bound cofactor S-adenosyl-L-methionine at 1.75 A each exhibit distinct relative positions of the substrate recognition and catalytic domains, revealing how PrmA can position the L11 substrate for multiple, consecutive side-chain methylation reactions. The fourth structure, the PrmA-L11 enzyme-substrate complex at 2.4 A resolution, illustrates the highly specific interaction of the N-terminal domain with its substrate and places Lys39 in the PrmA active site. The presence of a unique flexible loop in the cofactor-binding site suggests how exchange of AdoMet with the reaction product S-adenosyl-L-homocysteine can occur without necessitating the dissociation of PrmA from L11. Finally, the mode of interaction of PrmA with L11 explains its observed preference for L11 as substrate before its assembly into the 50S ribosomal subunit.
About this Structure
2NXN is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA., Demirci H, Gregory ST, Dahlberg AE, Jogl G, EMBO J. 2007 Jan 24;26(2):567-77. Epub 2007 Jan 11. PMID:17215866
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