1ps5
From Proteopedia
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| - | [[Image:1ps5.jpg|left|200px]] | ||
| - | + | ==STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION== | |
| - | + | <StructureSection load='1ps5' size='340' side='right'caption='[[1ps5]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | | | + | <table><tr><td colspan='2'>[[1ps5]] 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=1PS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PS5 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]] 2Å</td></tr> | |
| - | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ps5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps5 OCA], [https://pdbe.org/1ps5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ps5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ps5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ps5 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/ps/1ps5_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=1ps5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Suitable conditions for protein crystallization are commonly identified by screening combinations of independent factors that affect crystal formation. Because precipitating agents are prime determinants of crystallization, we investigated whether a systematic exploration of combinations of mechanistically distinct precipitants would enhance crystallization. A crystallization screen containing 64 precipitant mixtures was devised. Tests with ten HIV envelope-related proteins demonstrated that use of precipitant mixtures significantly enhanced both the probability of crystallization as well as the quality of optimized crystals. Tests with hen egg white lysozyme generated a novel C2 crystal from a salt/organic solvent mixture; structure solution at 2 A resolution revealed a lattice held together by both hydrophobic and electrostatic dyad interactions. The results indicate that mechanistically distinct precipitants can synergize, with precipitant combinations adding unique dimensions to protein crystallization. | ||
| - | + | Enhancing protein crystallization through precipitant synergy.,Majeed S, Ofek G, Belachew A, Huang CC, Zhou T, Kwong PD Structure. 2003 Sep;11(9):1061-70. PMID:12962625<ref>PMID:12962625</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1ps5" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | + | [[Category: Belachew A]] | |
| - | [[Category: Belachew | + | [[Category: Huang C]] |
| - | [[Category: Huang | + | [[Category: Kwong PD]] |
| - | [[Category: Kwong | + | [[Category: Majeed S]] |
| - | [[Category: Majeed | + | [[Category: Ofek G]] |
| - | [[Category: Ofek | + | [[Category: Zhou T]] |
| - | [[Category: Zhou | + | |
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Current revision
STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION
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Categories: Gallus gallus | Large Structures | Belachew A | Huang C | Kwong PD | Majeed S | Ofek G | Zhou T
