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3r26

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Perrhenate Binding to Molybdate Binding Protein

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Retrieved from "http://52.214.119.220/wiki/index.php/3r26"

Categories: Escherichia coli K-12 | Large Structures | Aryal BP | Brugarolas P | He C

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 <StructureSection load='3r26' size='340' side='right'caption='[[3r26]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3r26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R26 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3r26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R26 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=REO:PERRHENATE'>REO</scene></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]] 1.7&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">modA, b0763, JW0746 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=REO:PERRHENATE'>REO</scene></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=3r26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r26 OCA], [https://pdbe.org/3r26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r26 RCSB], [https://www.ebi.ac.uk/pdbsum/3r26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r26 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/MODA_ECOLI MODA_ECOLI]] Involved in the transport of molybdenum into the cell. Binds molybdate with high specificity and affinity.
+[https://www.uniprot.org/uniprot/MODA_ECOLI MODA_ECOLI] Involved in the transport of molybdenum into the cell. Binds molybdate with high specificity and affinity.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Radiolabeled biomolecules are routinely used for clinical diagnostics. (99m)Tc is the most commonly used radioactive tracer in radiopharmaceuticals. (188)Re and (186)Re are also commonly used as radioactive tracers in medicine. However, currently available methods for radiolabeling are lengthy and involve several steps in bioconjugation processes. In this work we present a strategy to engineer proteins that may selectively recognize the perrhenate (ReO(4) (-)) ion as a new way to label proteins. We found that a molybdate (MoO(4) (2-))-binding protein (ModA) from Escherichia coli can bind perrhenate with high affinity. Using fluorescence and isothermal titration calorimetry measurements, we determined the dissociation constant of ModA for ReO(4) (-) to be 541 nM and we solved a crystal structure of ModA with a bound ReO(4) (-). On the basis of the structure we created a mutant protein containing a disulfide linkage, which exhibited increased affinity for perrhenate (K (d) = 104 nM). High-resolution crystal structures of ModA (1.7 A) and A11C/R153C mutant (2.0 A) were solved with bound perrhenate. Both structures show that a perrhenate ion occupies the molybdate binding site using the same amino acid residues that are involved in molybdate binding. The overall structure of the perrhenate-bound ModA is unchanged compared with that of the molybdate-bound form. In the mutant protein, the bound perrhenate is further stabilized by the engineered disulfide bond.
-Binding of ReO(4) (-) with an engineered MoO (4) (2-)-binding protein: towards a new approach in radiopharmaceutical applications.,Aryal BP, Brugarolas P, He C J Biol Inorg Chem. 2012 Jan;17(1):97-106. Epub 2011 Aug 23. PMID:21861186<ref>PMID:21861186</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3r26" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[ABC transporter 3D structures|ABC transporter 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Aryal, B P]]
+[[Category: Aryal BP]]
-[[Category: Brugarolas, P]]
+[[Category: Brugarolas P]]
-[[Category: He, C]]
+[[Category: He C]]
-[[Category: Protein binding]]

3r26

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Perrhenate Binding to Molybdate Binding Protein

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