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<StructureSection load='1dd5' size='340' side='right'caption='[[1dd5]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='1dd5' size='340' side='right'caption='[[1dd5]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dd5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd5 OCA], [https://pdbe.org/1dd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd5 OCA], [https://pdbe.org/1dd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RRF_THEMA RRF_THEMA]] Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.  
[https://www.uniprot.org/uniprot/RRF_THEMA RRF_THEMA] Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dd5 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dd5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.,Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A Science. 1999 Dec 17;286(5448):2349-52. PMID:10600747<ref>PMID:10600747</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dd5" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribosome recycling factor|Ribosome recycling factor]]
*[[Ribosome recycling factor|Ribosome recycling factor]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Al-Karadaghi, S]]
[[Category: Thermotoga maritima]]
[[Category: Hirokawa, G]]
[[Category: Al-Karadaghi S]]
[[Category: Kaji, A]]
[[Category: Hirokawa G]]
[[Category: Liljas, A]]
[[Category: Kaji A]]
[[Category: Selmer, M]]
[[Category: Liljas A]]
[[Category: Beta-alpha-beta sandwich]]
[[Category: Selmer M]]
[[Category: Ribosome]]
[[Category: Three-helix bundle]]

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