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==Para-Arsanilate Derivative of Hen Egg-White Lysozyme== | |||
<StructureSection load='1n4f' size='340' side='right'caption='[[1n4f]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1n4f]] 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=1N4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4F 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]] 1.78Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASR:4-AMINOPHENYLARSONIC+ACID'>ASR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1n4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4f OCA], [https://pdbe.org/1n4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4f RCSB], [https://www.ebi.ac.uk/pdbsum/1n4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4f ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[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/n4/1n4f_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=1n4f ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Single/multiple-wavelength anomalous dispersion (SAD/MAD) experiments were performed on a crystal of an organic arsenic derivative of hen egg-white lysozyme. A para-arsanilate compound used as a crystallizing reagent was incorporated into the ordered solvent region of the lysozyme molecule. Diffraction data were collected to high resolution (</=2.0 A) at three wavelengths around the K edge (1.04 A) of arsenic at beamline BM30A, ESRF synchrotron. Anomalous Patterson maps clearly showed the main arsanilate site to be between three symmetry-related lysozyme molecules, at a location previously occupied by a para-toluenesulfonate anion. MAD phases at 2 A derived using the program SHARP led to an electron-density map of sufficient quality to start manual building of the protein model. Amplitudes from a second crystal measured to a resolution of 1.8 A at the peak wavelength revealed two additional heavy-atom sites, which reinforced the anomalous subset model and therefore dramatically improved the phasing power of the arsenic derivative. The subsequent solvent-flattened map was of such high accuracy that the program ARP/wARP was able to build a nearly complete model automatically. This work emphasizes the great potential of arsenic for de novo structure determination using anomalous dispersion methods. | |||
Phasing power at the K absorption edge of organic arsenic.,Retailleau P, Prange T Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):887-96. Epub 2003, Apr 25. PMID:12777806<ref>PMID:12777806</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1n4f" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Lysozyme 3D structures|Lysozyme 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Prange T]] | |||
[[Category: Prange | [[Category: Retailleau P]] | ||
[[Category: Retailleau | |||
Latest revision as of 10:22, 9 October 2024
Para-Arsanilate Derivative of Hen Egg-White LysozymePara-Arsanilate Derivative of Hen Egg-White Lysozyme
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 PubMedSingle/multiple-wavelength anomalous dispersion (SAD/MAD) experiments were performed on a crystal of an organic arsenic derivative of hen egg-white lysozyme. A para-arsanilate compound used as a crystallizing reagent was incorporated into the ordered solvent region of the lysozyme molecule. Diffraction data were collected to high resolution (</=2.0 A) at three wavelengths around the K edge (1.04 A) of arsenic at beamline BM30A, ESRF synchrotron. Anomalous Patterson maps clearly showed the main arsanilate site to be between three symmetry-related lysozyme molecules, at a location previously occupied by a para-toluenesulfonate anion. MAD phases at 2 A derived using the program SHARP led to an electron-density map of sufficient quality to start manual building of the protein model. Amplitudes from a second crystal measured to a resolution of 1.8 A at the peak wavelength revealed two additional heavy-atom sites, which reinforced the anomalous subset model and therefore dramatically improved the phasing power of the arsenic derivative. The subsequent solvent-flattened map was of such high accuracy that the program ARP/wARP was able to build a nearly complete model automatically. This work emphasizes the great potential of arsenic for de novo structure determination using anomalous dispersion methods. Phasing power at the K absorption edge of organic arsenic.,Retailleau P, Prange T Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):887-96. Epub 2003, Apr 25. PMID:12777806[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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