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3cjs

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Revision as of 13:16, 7 November 2018

Minimal Recognition Complex between PrmA and Ribosomal Protein L11

Structural highlights

3cjs is a 3 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2nxc, 2nxe, 2nxj, 2nxn, 1ufk, 3cjq, 3cjr, 3cjt, 3cju
Gene:	prmA (Thermus thermophilus), rplK, rpl11 (Thermus thermophilus)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRMA_THET8] Methylates ribosomal protein L11; this reaction probably occurs before the protein is assembled into the ribosome. This function is dispensable for growth and thermostability. [RL11_THETH] This protein binds directly to 23S ribosomal RNA (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.

Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.,Demirci H, Gregory ST, Dahlberg AE, Jogl G Structure. 2008 Jul;16(7):1059-66. PMID:18611379^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Demirci H, Gregory ST, Dahlberg AE, Jogl G. Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Structure. 2008 Jul;16(7):1059-66. PMID:18611379 doi:10.1016/j.str.2008.03.016

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cjs"

@@ Line 1: / Line 1: @@
 ==Minimal Recognition Complex between PrmA and Ribosomal Protein L11==
 <StructureSection load='3cjs' size='340' side='right' caption='[[3cjs]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nxc|2nxc]], [[2nxe|2nxe]], [[2nxj|2nxj]], [[2nxn|2nxn]], [[1ufk|1ufk]], [[3cjq|3cjq]], [[3cjr|3cjr]], [[3cjt|3cjt]], [[3cju|3cju]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prmA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]), rplK, rpl11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjs OCA], [http://pdbe.org/3cjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cjs RCSB], [http://www.ebi.ac.uk/pdbsum/3cjs PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cjs OCA], [http://pdbe.org/3cjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cjs RCSB], [http://www.ebi.ac.uk/pdbsum/3cjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cjs ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/3cjs_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/3cjs_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3cjs

From Proteopedia

Revision as of 13:16, 7 November 2018

Minimal Recognition Complex between PrmA and Ribosomal Protein L11

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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