1x1l
From Proteopedia
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|PDB= 1x1l |SIZE=350|CAPTION= <scene name='initialview01'>1x1l</scene> | |PDB= 1x1l |SIZE=350|CAPTION= <scene name='initialview01'>1x1l</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fjf|1FJF]], [[1ega|1EGA]], [[1wf3|1WF3]], [[1x18|1X18]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x1l OCA], [http://www.ebi.ac.uk/pdbsum/1x1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x1l RCSB]</span> | ||
}} | }} | ||
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[[Category: interaction of era protein with the 3'minor domain of 16s rrna]] | [[Category: interaction of era protein with the 3'minor domain of 16s rrna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:39 2008'' |
Revision as of 21:43, 30 March 2008
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| Ligands: | , , , | ||||||
| Related: | 1FJF, 1EGA, 1WF3, 1X18
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Interaction of ERA,a GTPase protein, with the 3'minor domain of the 16S rRNA within the THERMUS THERMOPHILUS 30S subunit.
Overview
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.
About this Structure
1X1L is a Single protein structure of sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 00:43:39 2008
