5jn6
From Proteopedia
(Difference between revisions)
m (Protected "5jn6" [edit=sysop:move=sysop]) |
|||
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5jn6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JN6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5jn6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JN6 FirstGlance]. <br> | ||
| - | </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=5jn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jn6 OCA], [http://pdbe.org/5jn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jn6 RCSB], [http://www.ebi.ac.uk/pdbsum/5jn6 PDBsum]</span></td></tr> | + | </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=5jn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jn6 OCA], [http://pdbe.org/5jn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jn6 RCSB], [http://www.ebi.ac.uk/pdbsum/5jn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jn6 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein function elucidation often relies heavily on amino acid sequence analysis and other bioinformatics approaches. The reliance is extended to structure homology modeling for ligand docking and protein-protein interaction mapping. However, sequence analysis of RPA3313 exposes a large, unannotated class of hypothetical proteins mostly from the Rhizobiales order. In the absence of sequence and structure information, further functional elucidation of this class of proteins has been significantly hindered. A high quality NMR structure of RPA3313 reveals that the protein forms a novel split betabetaalphabeta fold with a conserved ligand binding pocket between the first beta-strand and the N-terminus of the alpha-helix. Conserved residue analysis and protein-protein interaction prediction analyses reveal multiple protein binding sites and conserved functional residues. Results of a mass spectrometry proteomic analysis strongly point toward interaction with the ribosome and its subunits. The combined structural and proteomic analyses suggest that RPA3313 by itself or in a larger complex may assist in the transportation of substrates to or from the ribosome for further processing. Proteins 2016. (c) 2016 Wiley Periodicals, Inc. | ||
| + | |||
| + | The NMR solution structure and function of RPA3313: a putative ribosomal transport protein from Rhodopseudomonas palustris.,Catazaro J, Lowe AJ, Cerny RL, Powers R Proteins. 2016 Nov 1. doi: 10.1002/prot.25201. PMID:27802574<ref>PMID:27802574</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jn6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 03:38, 10 December 2016
The NMR Solution Structure of RPA3313
| |||||||||||
