2nxc: Difference between revisions
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[[Image:2nxc.gif|left|200px]] | [[Image:2nxc.gif|left|200px]] | ||
'''Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)''' | {{Structure | ||
|PDB= 2nxc |SIZE=350|CAPTION= <scene name='initialview01'>2nxc</scene>, resolution 1.59Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= prmA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |||
}} | |||
'''Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NXC is a [ | 2NXC is a [[Single protein]] structure of sequence 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=2NXC OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17215866 17215866] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: transferase s-adenosly-l-methionine dependent methyltransferase posttranslational modification]] | [[Category: transferase s-adenosly-l-methionine dependent methyltransferase posttranslational modification]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:52:22 2008'' | ||
Revision as of 18:52, 20 March 2008
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| , resolution 1.59Å | |||||||
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| Gene: | prmA (Thermus thermophilus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Apo-form of T. thermophilus ribosomal protein L11 methyltransferase (PrmA)
OverviewOverview
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 StructureAbout this Structure
2NXC is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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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