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New page: left|200px<br /><applet load="2eql" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eql, resolution 2.5Å" /> '''CRYSTALLOGRAPHIC STUD... |
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== | ==CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION== | ||
The crystal structure of a calcium binding equine lysozyme has been | <StructureSection load='2eql' size='340' side='right'caption='[[2eql]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2eql]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EQL FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2eql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eql OCA], [https://pdbe.org/2eql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eql RCSB], [https://www.ebi.ac.uk/pdbsum/2eql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eql ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LYSC1_HORSE LYSC1_HORSE] 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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eq/2eql_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2eql ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures. | |||
Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.,Tsuge H, Ago H, Noma M, Nitta K, Sugai S, Miyano M J Biochem. 1992 Feb;111(2):141-3. PMID:1569037<ref>PMID:1569037</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2eql" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ago | [[Category: Ago H]] | ||
[[Category: Miyano | [[Category: Miyano M]] | ||
[[Category: Tsuge | [[Category: Tsuge H]] | ||
Latest revision as of 03:53, 21 November 2024
CRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTIONCRYSTALLOGRAPHIC STUDIES OF A CALCIUM BINDING LYSOZYME FROM EQUINE MILK AT 2.5 ANGSTROMS RESOLUTION
Structural highlights
FunctionLYSC1_HORSE 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. 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 PubMedThe crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures. Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.,Tsuge H, Ago H, Noma M, Nitta K, Sugai S, Miyano M J Biochem. 1992 Feb;111(2):141-3. PMID:1569037[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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