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| | <StructureSection load='1xbi' size='340' side='right'caption='[[1xbi]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='1xbi' size='340' side='right'caption='[[1xbi]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xbi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XBI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xbi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XBI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 1.45Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPL7AE, MJ1203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=1xbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbi OCA], [http://pdbe.org/1xbi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xbi RCSB], [http://www.ebi.ac.uk/pdbsum/1xbi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbi 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=1xbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xbi OCA], [https://pdbe.org/1xbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xbi RCSB], [https://www.ebi.ac.uk/pdbsum/1xbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xbi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RL7A_METJA RL7A_METJA]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. | + | [https://www.uniprot.org/uniprot/RL7A_METJA RL7A_METJA] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 43067]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: II, B A.Brown]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Lieberman, D V]] | + | [[Category: Brown II BA]] |
| - | [[Category: Maxwell, E S]] | + | [[Category: Lieberman DV]] |
| - | [[Category: Suryadi, J]] | + | [[Category: Maxwell ES]] |
| - | [[Category: Tran, E J]] | + | [[Category: Suryadi J]] |
| - | [[Category: Alpha-beta-alpha sandwich fold]] | + | [[Category: Tran EJ]] |
| - | [[Category: Rna binding protein-structural protein complex]]
| + | |
| Structural highlights
Function
RL7A_METJA Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.
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
Archaeal ribosomal protein L7Ae is a multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal, box H/ACA, and box C/D sRNAs. The crystal structure of Methanocaldococcus jannaschii L7Ae has been determined to 1.45 A, and L7Ae's amino acid composition, evolutionary conservation, functional characteristics, and structural details have been analyzed. Comparison of the L7Ae structure to those of a number of related proteins with diverse functions has revealed significant structural homology which suggests that this protein fold is an ancient RNA-binding motif. Notably, the free M. jannaschii L7Ae structure is essentially identical to that with RNA bound, suggesting that RNA binding occurs through an induced-fit interaction. Circular dichroism experiments show that box C/D and C'/D' RNA motifs undergo conformational changes when magnesium or the L7Ae protein is added, corroborating the induced-fit model for L7Ae-box C/D RNA interactions.
The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs.,Suryadi J, Tran EJ, Maxwell ES, Brown BA 2nd Biochemistry. 2005 Jul 19;44(28):9657-72. PMID:16008351[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suryadi J, Tran EJ, Maxwell ES, Brown BA 2nd. The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs. Biochemistry. 2005 Jul 19;44(28):9657-72. PMID:16008351 doi:http://dx.doi.org/10.1021/bi050568q
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