2y32: Difference between revisions
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<StructureSection load='2y32' size='340' side='right' caption='[[2y32]], [[Resolution|resolution]] 1.78Å' scene=''> | <StructureSection load='2y32' size='340' side='right' caption='[[2y32]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
== Structural highlights == | == 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]. | <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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y32 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=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> | |||
<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> | ||
<table> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: Airenne, T T | [[Category: Airenne, T T]] | ||
[[Category: Gronroos, T | [[Category: Gronroos, T]] | ||
[[Category: Hytonen, V P | [[Category: Hytonen, V P]] | ||
[[Category: Johnson, M S | [[Category: Johnson, M S]] | ||
[[Category: Kulomaa, M S | [[Category: Kulomaa, M S]] | ||
[[Category: Leppiniemi, J | [[Category: Leppiniemi, J]] | ||
[[Category: Biotin-binding protein]] | [[Category: Biotin-binding protein]] | ||
Revision as of 02:23, 4 January 2015
Crystal structure of bradavidinCrystal structure of bradavidin
Structural highlights
Publication Abstract from PubMedBradavidin 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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