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2y32
From Proteopedia
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| - | [[ | + | ==Crystal structure of bradavidin== |
| + | <StructureSection load='2y32' size='340' side='right' caption='[[2y32]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2y32]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y32 OCA]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y32 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y32 RCSB], [http://www.ebi.ac.uk/pdbsum/2y32 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bradavidin is a homotetrameric biotin-binding protein from Bradyrhizobium japonicum, a nitrogen fixing and root nodule-forming symbiotic bacterium of the soybean. Wild-type (wt) bradavidin has 138 amino acid residues, whereas the C-terminally truncated core-bradavidin has only 118 residues. We have solved the X-ray structure of wt bradavidin and found that the C-terminal amino acids of each subunit were uniquely bound to the biotin-binding pocket of an adjacent subunit. The biotin-binding pocket occupying peptide (SEKLSNTK) was named "Brad-tag" and it serves as an intrinsic stabilizing ligand in wt bradavidin. The binding of Brad-tag to core-bradavidin was analysed by isothermal titration calorimetry and a binding affinity of approximately 25 microM was measured. In order to study the potential of Brad-tag, a green fluorescent protein tagged with Brad-tag was prepared and successfully concentrated from a bacterial cell lysate using core-bradavidin-functionalized Sepharose resin. | ||
| - | + | Structure of bradavidin - C-terminal residues act as intrinsic ligands.,Leppiniemi J, Gronroos T, Maatta JA, Johnson MS, Kulomaa MS, Hytonen VP, Airenne TT PLoS One. 2012;7(5):e35962. Epub 2012 May 4. PMID:22574129<ref>PMID:22574129</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: Airenne, T T.]] | [[Category: Airenne, T T.]] | ||
Revision as of 07:52, 14 May 2014
Crystal structure of bradavidin
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