|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='4pru' size='340' side='right'caption='[[4pru]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4pru' size='340' side='right'caption='[[4pru]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4pru]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PRU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4pru]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PRU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=T3Y:25,26,27,28-TETRAHYDROXYPENTACYCLO[19.3.1.1~3,7~.1~9,13~.1~15,19~]OCTACOSA-1(25),3(28),4,6,9(27),10,12,15(26),16,18,21,23-DODECAENE-5,11,17,23-TETRASULFONIC+ACID'>T3Y</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]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DM0:N~2~,N~2~,N~6~,N~6~-TETRAMETHYL-L-LYSINE'>DM0</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DM0:N~2~,N~2~,N~6~,N~6~-TETRAMETHYL-L-LYSINE'>DM0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=T3Y:25,26,27,28-TETRAHYDROXYPENTACYCLO[19.3.1.1~3,7~.1~9,13~.1~15,19~]OCTACOSA-1(25),3(28),4,6,9(27),10,12,15(26),16,18,21,23-DODECAENE-5,11,17,23-TETRASULFONIC+ACID'>T3Y</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n0j|4n0j]], [[4prq|4prq]]</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=4pru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pru OCA], [https://pdbe.org/4pru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pru RCSB], [https://www.ebi.ac.uk/pdbsum/4pru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pru ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=4pru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pru OCA], [http://pdbe.org/4pru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pru RCSB], [http://www.ebi.ac.uk/pdbsum/4pru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pru ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK]] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | + | [https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 30: |
Line 28: |
| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Crowley PB]] |
| - | [[Category: Crowley, P B]] | + | [[Category: Lyons JA]] |
| - | [[Category: Lyons, J A]] | + | [[Category: McGovern RE]] |
| - | [[Category: McGovern, R E]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
LYSC_CHICK Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]
Publication Abstract from PubMed
Lysine is a ubiquitous residue on protein surfaces. Post translational modifications of lysine, including methylation to the mono-, di- or trimethylated amine result in chemical and structural alterations that have major consequences for protein interactions and signalling pathways. Small molecules that bind to methylated lysines are potential tools to modify such pathways. To make progress in this direction, detailed structural data of ligands in complex with methylated lysine is required. Here, we report a crystal structure of p-sulfonatocalix[4]arene (sclx4) bound to methylated lysozyme in which the lysine residues were chemically modified from Lys-NH3 + to Lys-NH(Me2)+. Of the six possible dimethyllysine sites, sclx4 selected Lys116-Me2 and the dimethylamino substituent was deeply buried in the calixarene cavity. This complex confirms the tendency for Lys-Me2 residues to form cation-pi interactions, which have been shown to be important in protein recognition of histone tails bearing methylated lysines. Supporting data from NMR spectroscopy and MD simulations confirm the selectivity for Lys116-Me2 in solution. The structure presented here may serve as a stepping stone to the development of new biochemical reagents that target methylated lysines.
Structural study of a small molecule receptor bound to dimethyllysine in lysozyme.,McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I, Hof F, Crowley PB Chem Sci. 2015 Jan 1;6(1):442-449. PMID:25530835[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
- ↑ McGovern RE, Snarr BD, Lyons JA, McFarlane J, Whiting AL, Paci I, Hof F, Crowley PB. Structural study of a small molecule receptor bound to dimethyllysine in lysozyme. Chem Sci. 2015 Jan 1;6(1):442-449. PMID:25530835 doi:http://dx.doi.org/10.1039/C4SC02383H
|
