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[[Image:1ps5.jpg|left|200px]]


{{Structure
==STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION==
|PDB= 1ps5 |SIZE=350|CAPTION= <scene name='initialview01'>1ps5</scene>, resolution 2.00&Aring;
<StructureSection load='1ps5' size='340' side='right'caption='[[1ps5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<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>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
</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&#8491;</td></tr>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ps5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ps5 OCA], [http://www.ebi.ac.uk/pdbsum/1ps5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ps5 RCSB]</span>
== 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.


'''STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION'''
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ps5" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==About this Structure==
<references/>
1PS5 is a [[Single protein]] structure of sequence from [http://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].
__TOC__
 
</StructureSection>
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12962625 12962625]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Belachew A]]
[[Category: Belachew, A.]]
[[Category: Huang C]]
[[Category: Huang, C.]]
[[Category: Kwong PD]]
[[Category: Kwong, P D.]]
[[Category: Majeed S]]
[[Category: Majeed, S.]]
[[Category: Ofek G]]
[[Category: Ofek, G.]]
[[Category: Zhou T]]
[[Category: Zhou, T.]]
[[Category: glycosidase]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:03:50 2008''

Latest revision as of 11:44, 6 November 2024

STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTIONSTRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG-WHITE LYSOZYME AT 2.0 ANGSTROMS RESOLUTION

Structural highlights

1ps5 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[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 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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. ↑ Majeed S, Ofek G, Belachew A, Huang CC, Zhou T, Kwong PD. Enhancing protein crystallization through precipitant synergy. Structure. 2003 Sep;11(9):1061-70. PMID:12962625

1ps5, resolution 2.00Å

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