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| <StructureSection load='7kh5' size='340' side='right'caption='[[7kh5]], [[Resolution|resolution]] 1.29Å' scene=''> | | <StructureSection load='7kh5' size='340' side='right'caption='[[7kh5]], [[Resolution|resolution]] 1.29Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7kh5]] 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=7KH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KH5 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KH5 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WE4:2,3,5,6-tetrabromobenzene-1,4-dicarboxylic+acid'>WE4</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]] 1.295Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://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=WE4:2,3,5,6-tetrabromobenzene-1,4-dicarboxylic+acid'>WE4</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=7kh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kh5 OCA], [https://pdbe.org/7kh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kh5 RCSB], [https://www.ebi.ac.uk/pdbsum/7kh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kh5 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=7kh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kh5 OCA], [https://pdbe.org/7kh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kh5 RCSB], [https://www.ebi.ac.uk/pdbsum/7kh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kh5 ProSAT]</span></td></tr> |
| </table> | | </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>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The phase problem is a persistent bottleneck that impedes the structure-determination pipeline and must be solved to obtain atomic resolution crystal structures of macromolecules. Although molecular replacement has become the predominant method of solving the phase problem, many scenarios still exist in which experimental phasing is needed. Here, a proof-of-concept study is presented that shows the efficacy of using tetrabromoterephthalic acid (B4C) as an experimental phasing compound. Incorporating B4C into the crystal lattice using co-crystallization, the crystal structure of hen egg-white lysozyme was solved using MAD phasing. The strong anomalous signal generated by its four Br atoms coupled with its compatibility with commonly used crystallization reagents render B4C an effective experimental phasing compound that can be used to overcome the phase problem.
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| Simplified heavy-atom derivatization of protein structures via co-crystallization with the MAD tetragon tetrabromoterephthalic acid.,Truong JQ, Nguyen S, Bruning JB, Shearwin KE Acta Crystallogr F Struct Biol Commun. 2021 May 1;77(Pt 5):156-162. doi:, 10.1107/S2053230X21004052. Epub 2021 Apr 28. PMID:33949976<ref>PMID:33949976</ref>
| | ==See Also== |
| | | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7kh5" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Gallus gallus]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lysozyme]]
| | [[Category: Nguyen S]] |
| [[Category: Nguyen, S]] | | [[Category: Truong J]] |
| [[Category: Truong, J]] | |
| [[Category: Antimicrobial protein]]
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| [[Category: Hydrolase]]
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| [[Category: Lyzozyme]]
| |