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4xlc

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==Tailspike protein double mutant D339N/E372A of E. coli bacteriophage HK620==
==Tailspike protein double mutant D339N/E372A of E. coli bacteriophage HK620==
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<StructureSection load='4xlc' size='340' side='right' caption='[[4xlc]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='4xlc' size='340' side='right'caption='[[4xlc]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4xlc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XLC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4xlc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_HK620 Enterobacteria phage HK620]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<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=4xlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlc OCA], [http://pdbe.org/4xlc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xlc RCSB], [http://www.ebi.ac.uk/pdbsum/4xlc PDBsum]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlc OCA], [https://pdbe.org/4xlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xlc RCSB], [https://www.ebi.ac.uk/pdbsum/4xlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlc ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9AYY6_BPHK6 Q9AYY6_BPHK6]
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Bacteriophage HK620 recognizes and cleaves the Oantigen polysaccharide of E. coli serogroup O18A1 with its tailspike protein (TSP). HK620TSP binds hexasaccharide fragments with low affinity, but single amino acid exchanges generated a set of high-affinity mutants with submicromolar dissociation constants. Isothermal titration calorimetry showed that only small amounts of heat were released upon complex formation via a large number of direct and solvent mediated hydrogen bonds between carbohydrate and protein. At room temperature association was both enthalpy- and entropy-driven emphasizing major solvent rearrangements upon complex formation. Crystal structure analysis showed identical protein and sugar conformers in the TSP complexes regardless of their hexasaccharide affinity. Only in one case a TSP mutant bound a different hexasaccharide conformer. The extended sugar binding site could be dissected in two regions: Firstly, a hydrophobic pocket at the reducing end with minor affinity contributions. Access to this site could be blocked by a single aspartate to asparagine exchange without major loss in hexasaccharide affinity. Secondly, a region where specific exchange of glutamate for glutamine created a site for an additional water molecule. Side chain rearrangements upon sugar binding led to desolvation and additional hydrogen bonding which define this region of the binding site as the high affinity scaffold.
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Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity.,Broeker NK, Gohlke U, Muller JJ, Uetrecht C, Heinemann U, Seckler R, Barbirz S Glycobiology. 2012 Aug 24. PMID:22923442<ref>PMID:22923442</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Tailspike protein 3D structures|Tailspike protein 3D structures]]
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<div class="pdbe-citations 4xlc" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Barbirz, S]]
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[[Category: Enterobacteria phage HK620]]
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[[Category: Broeker, N K]]
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[[Category: Large Structures]]
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[[Category: Gohlke, U]]
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[[Category: Barbirz S]]
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[[Category: Heinemann, U]]
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[[Category: Broeker NK]]
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[[Category: Seckler, R]]
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[[Category: Gohlke U]]
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[[Category: Beta helix]]
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[[Category: Heinemann U]]
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[[Category: Pectin lyase fold]]
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[[Category: Seckler R]]
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[[Category: Protein-carbohydrate complex]]
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[[Category: Viral protein]]
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Current revision

Tailspike protein double mutant D339N/E372A of E. coli bacteriophage HK620

PDB ID 4xlc

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