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1lzt
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lzt' size='340' side='right'caption='[[1lzt]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='1lzt' size='340' side='right'caption='[[1lzt]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lzt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1lzt]] 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=1LZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LZT 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">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</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=1lzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzt OCA], [https://pdbe.org/1lzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzt RCSB], [https://www.ebi.ac.uk/pdbsum/1lzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzt 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=1lzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lzt OCA], [https://pdbe.org/1lzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lzt RCSB], [https://www.ebi.ac.uk/pdbsum/1lzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lzt 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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</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=1lzt ConSurf]. | </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=1lzt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | X-ray diffraction data to 1.5 A resolution have been collected for triclinic crystals of hen egg white lysozyme. The triclinic model was derived from the tetragonal one by the rotation function and refined initially by Fo-Fc and differential difference syntheses against 2 A resolution data. Refinement was continued by differential difference cycles against the 1.5 A data until R was reduced to 0.220. Although the initial refinement was rapid, it was subsequently a matter of attrition, leading to a complete recheck of the data and the discovery of systematic error which affected primarily the high-resolution data. Refinement was continued against the corrected 2 A data by block-diagonal least squares. After five cycles the refinement was terminated at R = 0.254 because of the imminent availability of a preferred refinement program. Problems with the protein model, the solvent, and the interaction of the scale and thermal parameters are discussed. The experiences gained in this study are summarized. | ||
| - | |||
| - | Refinement of triclinic lysozyme: I. Fourier and least-squares methods.,Hodsdon JM, Brown GM, Sieker LC, Jensen LH Acta Crystallogr B. 1990 Feb 1;46 ( Pt 1):54-62. PMID:2302326<ref>PMID:2302326</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1lzt" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Gallus gallus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Brown GM]] | |
| - | [[Category: Brown | + | [[Category: Hodsdon JM]] |
| - | [[Category: Hodsdon | + | [[Category: Jensen LH]] |
| - | [[Category: Jensen | + | [[Category: Sieker LC]] |
| - | [[Category: Sieker | + | |
Current revision
REFINEMENT OF TRICLINIC LYSOZYME
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