2y32: Difference between revisions
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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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2Y32 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78Å</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=2y32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y32 OCA], [https://pdbe.org/2y32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y32 RCSB], [https://www.ebi.ac.uk/pdbsum/2y32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y32 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q89IH6_BRADU Q89IH6_BRADU] | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2y32" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bradyrhizobium japonicum]] | |||
[[Category: Large Structures]] | |||
[[Category: Airenne TT]] | |||
[[Category: Gronroos T]] | |||
[[Category: Hytonen VP]] | |||
[[Category: Johnson MS]] | |||
[[Category: Kulomaa MS]] | |||
[[Category: Leppiniemi J]] | |||
Latest revision as of 11:07, 23 August 2023
Crystal structure of bradavidinCrystal structure of bradavidin
Structural highlights
FunctionPublication 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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