1dd5

From Proteopedia

(Difference between revisions)

Revision as of 09:50, 15 September 2021

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF

Structural highlights

1dd5 is a 1 chain structure with sequence from Atcc 43589. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

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

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^[1]

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

References

↑ Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A. Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science. 1999 Dec 17;286(5448):2349-52. PMID:10600747

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/1dd5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1dd5' size='340' side='right'caption='[[1dd5]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dd5]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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/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>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene></td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd5 OCA], [http://pdbe.org/1dd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dd5 RCSB], [http://www.ebi.ac.uk/pdbsum/1dd5 PDBsum], [http://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>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1dd5

From Proteopedia

Revision as of 09:50, 15 September 2021

CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA RIBOSOME RECYCLING FACTOR, RRF

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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