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| ==Crystal structure of the colicin E2 DNase-Im2 complex== | | ==Crystal structure of the colicin E2 DNase-Im2 complex== |
| <StructureSection load='3u43' size='340' side='right' caption='[[3u43]], [[Resolution|resolution]] 1.72Å' scene=''> | | <StructureSection load='3u43' size='340' side='right'caption='[[3u43]], [[Resolution|resolution]] 1.72Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3u43]] is a 2 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=3U43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U43 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3u43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U43 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.72Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">imm, ceiB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), col, ceaB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3u43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u43 RCSB], [http://www.ebi.ac.uk/pdbsum/3u43 PDBsum]</span></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=3u43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u43 OCA], [https://pdbe.org/3u43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u43 RCSB], [https://www.ebi.ac.uk/pdbsum/3u43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u43 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/IMM2_ECOLX IMM2_ECOLX]] This protein is able to protect a cell, which harbors the plasmid ColE2 encoding colicin E2, against colicin E2. [[http://www.uniprot.org/uniprot/CEA2_ECOLX CEA2_ECOLX]] This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria. | | [https://www.uniprot.org/uniprot/IMM2_ECOLX IMM2_ECOLX] This protein is able to protect a cell, which harbors the plasmid ColE2 encoding colicin E2, against colicin E2. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| How proteins achieve high-affinity binding to a specific protein partner while simultaneously excluding all others is a major biological problem that has important implications for protein design. We report the crystal structure of the ultra-high-affinity protein-protein complex between the endonuclease domain of colicin E2 and its cognate immunity (Im) protein, Im2 (K(d) approximately 10(-)(15) M), which, by comparison to previous structural and biophysical data, provides unprecedented insight into how high affinity and selectivity are achieved in this model family of protein complexes. Our study pinpoints the role of structured water molecules in conjoining hotspot residues that govern stability with residues that control selectivity. A key finding is that a single residue, which in a noncognate context massively destabilizes the complex through frustration, does not participate in specificity directly but rather acts as an organizing center for a multitude of specificity interactions across the interface, many of which are water mediated.
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| Structure of the Ultra-High-Affinity Colicin E2 DNase-Im2 Complex.,Wojdyla JA, Fleishman SJ, Baker D, Kleanthous C J Mol Biol. 2012 Mar 16;417(1-2):79-94. Epub 2012 Jan 27. PMID:22306467<ref>PMID:22306467</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also== | | ==See Also== |
| *[[Colicin|Colicin]] | | *[[Colicin 3D structures|Colicin 3D structures]] |
| *[[Colicin Immunity Protein|Colicin Immunity Protein]] | | *[[Colicin immunity protein 3D structures|Colicin immunity protein 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| [[Category: Kleanthous, C]] | | [[Category: Large Structures]] |
| [[Category: Wojdyla, J A]] | | [[Category: Kleanthous C]] |
| [[Category: Dnase]] | | [[Category: Wojdyla JA]] |
| [[Category: High affinity]]
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| [[Category: Protein binding]]
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| [[Category: Protein-protein complex]]
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