3axf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3axf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXF FirstGlance]. <br> | <table><tr><td colspan='2'>[[3axf]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AXF FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=REO:PERRHENATE'>REO</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=REO:PERRHENATE'>REO</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r26|3r26]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3r26|3r26]]</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=3axf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3axf RCSB], [http://www.ebi.ac.uk/pdbsum/3axf PDBsum]</span></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=3axf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3axf RCSB], [http://www.ebi.ac.uk/pdbsum/3axf PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Aryal, B P | [[Category: Aryal, B P]] | ||
[[Category: Brugarolas, P | [[Category: Brugarolas, P]] | ||
[[Category: He, C | [[Category: He, C]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
[[Category: Molybdate binding protein]] | [[Category: Molybdate binding protein]] | ||
Revision as of 04:10, 25 December 2014
Perrhenate binding to A11C/R153C ModA mutantPerrhenate binding to A11C/R153C ModA mutant
Structural highlights
Function[MODA_ECOLI] Involved in the transport of molybdenum into the cell. Binds molybdate with high specificity and affinity. Publication Abstract from PubMedRadiolabeled 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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