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3ieu

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Revision as of 10:06, 19 December 2018

Crystal Structure of ERA in Complex with GDP

Structural highlights

3ieu is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1ega, 1wf3, 1x1l
Gene:	b2566, era, Escherichia coli, JW2550, rbaA (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ERA_ECOLI] An essential GTPase that binds both GDP and GTP, with nucleotide exchange occurring on the order of seconds whereas hydrolysis occurs on the order of minutes. Plays a role in numerous processes, including cell cycle regulation, energy metabolism, as a chaperone for 16S rRNA processing and 30S ribosomal subunit biogenesis. Its presence in the 30S subunit may prevent translation initiation. Seems to be critical for maintaining cell growth and cell divison rates; a dramatic reduction in Era protein levels temporarily arrests cell growth just before cytokinesis (at the predivisional two-cell stage) and delays cell division. Era mutant era1 suppresses some temperature-sensitive mutations that affect DNA replication and chromosome partitioning and segregation. The dominant-negative Era-de mutant which is missing residues in a putative effector region, is unable to complement the disruption mutant; upon overproduction it shows a significant decrease in cell viability and a synthetic lethal phenotype in the presence of acetate. Era function probably overlaps RbfA. Binds to the pre-30S subunit through several stages of protein assembly.^[1] ^[2] ^[3] ^[4] ^[5]

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

ERA, composed of an N-terminal GTPase domain followed by an RNA-binding KH domain, is essential for bacterial cell viability. It binds to 16S rRNA and the 30S ribosomal subunit. However, its RNA-binding site, the functional relationship between the two domains, and its role in ribosome biogenesis remain unclear. We have determined two crystal structures of ERA, a binary complex with GDP and a ternary complex with a GTP-analog and the 1531AUCACCUCCUUA1542 sequence at the 3' end of 16S rRNA. In the ternary complex, the first nine of the 12 nucleotides are recognized by the protein. We show that GTP binding is a prerequisite for RNA recognition by ERA and that RNA recognition stimulates its GTP-hydrolyzing activity. Based on these and other data, we propose a functional cycle of ERA, suggesting that the protein serves as a chaperone for processing and maturation of 16S rRNA and a checkpoint for assembly of the 30S ribosomal subunit. The AUCA sequence is highly conserved among bacteria, archaea, and eukaryotes, whereas the CCUCC, known as the anti-Shine-Dalgarno sequence, is conserved in noneukaryotes only. Therefore, these data suggest a common mechanism for a highly conserved ERA function in all three kingdoms of life by recognizing the AUCA, with a "twist" for noneukaryotic ERA proteins by also recognizing the CCUCC.

Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.,Tu C, Zhou X, Tropea JE, Austin BP, Waugh DS, Court DL, Ji X Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14843-8. Epub 2009 Aug 17. PMID:19706445^[6]

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

References

↑ Britton RA, Powell BS, Dasgupta S, Sun Q, Margolin W, Lupski JR, Court DL. Cell cycle arrest in Era GTPase mutants: a potential growth rate-regulated checkpoint in Escherichia coli. Mol Microbiol. 1998 Feb;27(4):739-50. PMID:9515700
↑ Inoue K, Chen J, Kato I, Inouye M. Specific growth inhibition by acetate of an Escherichia coli strain expressing Era-dE, a dominant negative Era mutant. J Mol Microbiol Biotechnol. 2002 Jul;4(4):379-88. PMID:12125819
↑ Inoue K, Alsina J, Chen J, Inouye M. Suppression of defective ribosome assembly in a rbfA deletion mutant by overexpression of Era, an essential GTPase in Escherichia coli. Mol Microbiol. 2003 May;48(4):1005-16. PMID:12753192
↑ Inoue K, Chen J, Tan Q, Inouye M. Era and RbfA have overlapping function in ribosome biogenesis in Escherichia coli. J Mol Microbiol Biotechnol. 2006;11(1-2):41-52. PMID:16825789 doi:10.1159/000092818
↑ Bunner AE, Nord S, Wikstrom PM, Williamson JR. The effect of ribosome assembly cofactors on in vitro 30S subunit reconstitution. J Mol Biol. 2010 Apr 23;398(1):1-7. doi: 10.1016/j.jmb.2010.02.036. Epub 2010 Feb, 24. PMID:20188109 doi:10.1016/j.jmb.2010.02.036
↑ Tu C, Zhou X, Tropea JE, Austin BP, Waugh DS, Court DL, Ji X. Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis. Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14843-8. Epub 2009 Aug 17. PMID:19706445

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/3ieu"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of ERA in Complex with GDP==
 <StructureSection load='3ieu' size='340' side='right' caption='[[3ieu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ega|1ega]], [[1wf3|1wf3]], [[1x1l|1x1l]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2566, era, Escherichia coli, JW2550, rbaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ieu OCA], [http://pdbe.org/3ieu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ieu RCSB], [http://www.ebi.ac.uk/pdbsum/3ieu 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=3ieu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ieu OCA], [http://pdbe.org/3ieu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ieu RCSB], [http://www.ebi.ac.uk/pdbsum/3ieu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ieu 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/ie/3ieu_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ie/3ieu_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3ieu

From Proteopedia

Revision as of 10:06, 19 December 2018

Crystal Structure of ERA in Complex with GDP

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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