1io5: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1io5]] 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=1IO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1io5]] 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=1IO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></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=1io5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io5 OCA], [https://pdbe.org/1io5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io5 RCSB], [https://www.ebi.ac.uk/pdbsum/1io5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io5 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=1io5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io5 OCA], [https://pdbe.org/1io5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io5 RCSB], [https://www.ebi.ac.uk/pdbsum/1io5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Castagna JC]] | |||
[[Category: Castagna | [[Category: Cipriani F]] | ||
[[Category: Cipriani | [[Category: Hoeghoej P]] | ||
[[Category: Hoeghoej | [[Category: Lehmann MS]] | ||
[[Category: Lehmann | [[Category: Minezaki Y]] | ||
[[Category: Minezaki | [[Category: Niimura N]] | ||
[[Category: Niimura | [[Category: Nonaka T]] | ||
[[Category: Nonaka | [[Category: Wilkinson C]] | ||
[[Category: Wilkinson | |||
Revision as of 10:10, 25 October 2023
HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTIONHYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINED BY NEUTRON DIFFRACTION
Structural highlights
FunctionLYSC_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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNeutron quasi-Laue diffraction data (2 A resolution) from tetragonal hen egg-white lysozyme were collected in ten days with neutron imaging plates. The data processing Laue software, LAUEGEN, developed for X-ray Laue diffractometry, was adapted for neutron diffractometry with a cylindrical detector. The data analysis software, X-PLOR, was modified and used for the refinement of hydrogen atoms, and the positions of 960 hydrogen atoms in the protein and 157 bound water molecules, were determined. Several examples are given of the methods used to identify hydrogen atoms and water molecules. Neutron Laue diffractometry with an imaging plate provides an effective data collection regime for neutron protein crystallography.,Niimura N, Minezaki Y, Nonaka T, Castagna JC, Cipriani F, Hoghoj P, Lehmann MS, Wilkinson C Nat Struct Biol. 1997 Nov;4(11):909-14. PMID:9360606[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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