2y32: Difference between revisions
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==Crystal structure of bradavidin== | ==Crystal structure of bradavidin== | ||
<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 [ | <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><td class="sblockLbl"><b> | </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q89IH6_BRADU Q89IH6_BRADU] | |||
<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> | ||
<div class="pdbe-citations 2y32" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: Airenne | [[Category: Large Structures]] | ||
[[Category: Gronroos | [[Category: Airenne TT]] | ||
[[Category: Hytonen | [[Category: Gronroos T]] | ||
[[Category: Johnson | [[Category: Hytonen VP]] | ||
[[Category: Kulomaa | [[Category: Johnson MS]] | ||
[[Category: Leppiniemi | [[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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