4ggt: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4ggt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_diazoefficiens_USDA_110 Bradyrhizobium diazoefficiens USDA 110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GGT FirstGlance]. <br>
-</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=4ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ggt OCA], [https://pdbe.org/4ggt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ggt RCSB], [https://www.ebi.ac.uk/pdbsum/4ggt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ggt ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.693&#8491;</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=4ggt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ggt OCA], [https://pdbe.org/4ggt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ggt RCSB], [https://www.ebi.ac.uk/pdbsum/4ggt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ggt ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q89U61_BRADU Q89U61_BRADU]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Bradavidin II is a biotin-binding protein from Bradyrhizobium japonicum that resembles chicken avidin and bacterial streptavidin. A biophysical characterization was carried out using dynamic light scattering, native mass spectrometry, differential scanning calorimetry, and isothermal titration calorimetry combined with structural characterization using X-ray crystallography. These observations revealed that bradavidin II differs from canonical homotetrameric avidin protein family members in its quaternary structure. In contrast with the other avidins, bradavidin II appears to have a dynamic (transient) oligomeric state in solution. It is monomeric at low protein concentrations but forms higher oligomeric assemblies at higher concentrations. The crystal structure of bradavidin II revealed an important role for Phe42 in shielding the bound ligand from surrounding water molecules, thus functionally replacing the L7,8 loop essential for tight ligand binding in avidin and streptavidin. This bradavidin II characterization opens new avenues for oligomerization-independent biotin-binding protein development.
-The highly dynamic oligomeric structure of bradavidin II is unique among avidin proteins.,Leppiniemi J, Meir A, Kahkonen N, Kukkurainen S, Maatta JA, Ojanen M, Janis J, S Kulomaa M, Livnah O, Hytonen VP Protein Sci. 2013 May 10. doi: 10.1002/pro.2281. PMID:23661323<ref>PMID:23661323</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ggt" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Avidin 3D structures|Avidin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>