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1x18

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Revision as of 16:42, 10 April 2020

Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT

1x18, resolution 13.50Å

Structural highlights

1x18 is a 9 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971 and Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1fjf, 1ega, 1wf3, 1x1l
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RS7_THET8] One of the primary rRNA binding proteins, it binds directly to 3'-end of the 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center. Binds mRNA and the E site tRNA blocking its exit path in the ribosome. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA.[HAMAP-Rule:MF_00480_B] [RS11_THET8] Located on the upper part of the platform of the 30S subunit, where it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it interacts both with the Shine-Dalgarno helix and mRNA.[HAMAP-Rule:MF_01310] [RS18_THETH] Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit (By similarity). [RS2_THET8] Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.[HAMAP-Rule:MF_00291_B]

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Era (E. coliRas-like protein) is a highly conserved and essential GTPase in bacteria. It binds to the 16S ribosomal RNA (rRNA) of the small (30S) ribosomal subunit, and its depletion leads to accumulation of an unprocessed precursor of the 16S rRNA. We have obtained a three-dimensional cryo-electron microscopic map of the Thermus thermophilus 30S-Era complex. Era binds in the cleft between the head and platform of the 30S subunit and locks the subunit in a conformation that is not favorable for association with the large (50S) ribosomal subunit. The RNA binding KH motif present within the C-terminal domain of Era interacts with the conserved nucleotides in the 3' region of the 16S rRNA. Furthermore, Era makes contact with several assembly elements of the 30S subunit. These observations suggest a direct involvement of Era in the assembly and maturation of the 30S subunit.

Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly.,Sharma MR, Barat C, Wilson DN, Booth TM, Kawazoe M, Hori-Takemoto C, Shirouzu M, Yokoyama S, Fucini P, Agrawal RK Mol Cell. 2005 Apr 29;18(3):319-29. PMID:15866174^[1]

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

References

↑ Sharma MR, Barat C, Wilson DN, Booth TM, Kawazoe M, Hori-Takemoto C, Shirouzu M, Yokoyama S, Fucini P, Agrawal RK. Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly. Mol Cell. 2005 Apr 29;18(3):319-29. PMID:15866174 doi:10.1016/j.molcel.2005.03.028

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/1x18"

@@ Line 3: / Line 3: @@
 <SX load='1x18' size='340' side='right' viewer='molstar' caption='[[1x18]], [[Resolution|resolution]] 13.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1x18]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1X18 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1x18]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971] and [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X18 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X18 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fjf|1fjf]], [[1ega|1ega]], [[1wf3|1wf3]], [[1x1l|1x1l]]</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=1x18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x18 OCA], [http://pdbe.org/1x18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x18 RCSB], [http://www.ebi.ac.uk/pdbsum/1x18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x18 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1x18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x18 OCA], [http://pdbe.org/1x18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x18 RCSB], [http://www.ebi.ac.uk/pdbsum/1x18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x18 ProSAT]</span></td></tr>
 </table>
 == Function ==

1x18

From Proteopedia

Revision as of 16:42, 10 April 2020

Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT

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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