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| | <StructureSection load='5nbj' size='340' side='right'caption='[[5nbj]], [[Resolution|resolution]] 1.27Å' scene=''> | | <StructureSection load='5nbj' size='340' side='right'caption='[[5nbj]], [[Resolution|resolution]] 1.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nbj]] is a 1 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=5NBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NBJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nbj]] is a 1 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=5NBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NBJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RE:RHENIUM'>RE</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]] 1.266Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RE:RHENIUM'>RE</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=5nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbj OCA], [http://pdbe.org/5nbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nbj RCSB], [http://www.ebi.ac.uk/pdbsum/5nbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbj 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=5nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nbj OCA], [https://pdbe.org/5nbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nbj RCSB], [https://www.ebi.ac.uk/pdbsum/5nbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nbj 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 == |
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| | [[Category: Gallus gallus]] | | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysozyme]]
| + | [[Category: Brink A]] |
| - | [[Category: Brink, A]] | + | [[Category: Helliwell JR]] |
| - | [[Category: Helliwell, J R]] | + | |
| - | [[Category: Hen egg white lysozyme]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Radiopharmaceutical development]]
| + | |
| - | [[Category: Rhenium tricarbonyl]]
| + | |
| 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
Multiple possibilities for the coordination of fac-[Re(CO)3(H2O)3]+ to a protein have been determined and include binding to Asp, Glu, Arg and His amino-acid residues as well as to the C-terminal carboxylate in the vicinity of Leu and Pro. The large number of rhenium metal complex binding sites that have been identified on specific residues thereby allow increased target identification for the design of future radiopharmaceuticals. The core experimental concept involved the use of state-of-art tuneable synchrotron radiation at the Diamond Light Source to optimize the rhenium anomalous dispersion signal to a large value (f of 12.1 electrons) at its LI absorption edge with a selected X-ray wavelength of 0.9763 A. At the Cu Kalpha X-ray wavelength (1.5418 A) the f for rhenium is 5.9 electrons. The expected peak-height increase owing to the optimization of the Re f was therefore 2.1. This X-ray wavelength tuning methodology thereby showed the lower occupancy rhenium binding sites as well as the occupancies of the higher occupancy rhenium binding sites.
New leads for fragment-based design of rhenium/technetium radiopharmaceutical agents.,Brink A, Helliwell JR IUCrJ. 2017 Apr 11;4(Pt 3):283-290. doi: 10.1107/S2052252517003475. eCollection, 2017 May 1. PMID:28512575[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
- ↑ Brink A, Helliwell JR. New leads for fragment-based design of rhenium/technetium radiopharmaceutical agents. IUCrJ. 2017 Apr 11;4(Pt 3):283-290. doi: 10.1107/S2052252517003475. eCollection, 2017 May 1. PMID:28512575 doi:http://dx.doi.org/10.1107/S2052252517003475
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