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| | <StructureSection load='2x6w' size='340' side='right'caption='[[2x6w]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='2x6w' size='340' side='right'caption='[[2x6w]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bphk6 Bphk6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X6W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X6W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x6w]] 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=2X6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X6W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x85|2x85]], [[2x6y|2x6y]], [[2vji|2vji]], [[2x6x|2x6x]], [[2vjj|2vjj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2x6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x6w OCA], [http://pdbe.org/2x6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x6w RCSB], [http://www.ebi.ac.uk/pdbsum/2x6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x6w ProSAT]</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=2x6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x6w OCA], [https://pdbe.org/2x6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x6w RCSB], [https://www.ebi.ac.uk/pdbsum/2x6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x6w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9AYY6_BPHK6 Q9AYY6_BPHK6] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Tailspike protein|Tailspike protein]] | + | *[[Tailspike protein 3D structures|Tailspike protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bphk6]] | + | [[Category: Enterobacteria phage HK620]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barbirz, S]] | + | [[Category: Barbirz S]] |
| - | [[Category: Heinemann, U]] | + | [[Category: Heinemann U]] |
| - | [[Category: Lorenzen, N K]] | + | [[Category: Lorenzen NK]] |
| - | [[Category: Mueller, J J]] | + | [[Category: Mueller JJ]] |
| - | [[Category: Seckler, R]] | + | [[Category: Seckler R]] |
| - | [[Category: Beta-helix]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
2x6w is a 1 chain structure with sequence from Enterobacteria phage HK620. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.35Å |
| Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q9AYY6_BPHK6
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Broeker NK, Gohlke U, Muller JJ, Uetrecht C, Heinemann U, Seckler R, Barbirz S. Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity. Glycobiology. 2012 Aug 24. PMID:22923442 doi:http://dx.doi.org/10.1093/glycob/cws126
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