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[[Image:1lsd.jpg|left|200px]]
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{{STRUCTURE_1lsd|  PDB=1lsd  |  SCENE=  }}
'''THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER'''


==THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER==
<StructureSection load='1lsd' size='340' side='right'caption='[[1lsd]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lsd]] 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=1LSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LSD 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]] 1.7&#8491;</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=1lsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsd OCA], [https://pdbe.org/1lsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lsd RCSB], [https://www.ebi.ac.uk/pdbsum/1lsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsd 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/ls/1lsd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1lsd ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 A(3) from 295 to 250 K and about 220 200 A(3) below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondary-structure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hinge-bending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.


==Overview==
The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water.,Kurinov IV, Harrison RW Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):98-109. PMID:15299341<ref>PMID:15299341</ref>
Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 A(3) from 295 to 250 K and about 220 200 A(3) below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondary-structure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hinge-bending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1LSD 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=1LSD OCA].
</div>
<div class="pdbe-citations 1lsd" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water., Kurinov IV, Harrison RW, Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):98-109. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299341 15299341]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Harrison RW]]
[[Category: Harrison, R W.]]
[[Category: Kurinov I]]
[[Category: Kurinov, I.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:14:28 2008''

Latest revision as of 08:31, 5 June 2024

THE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATERTHE INFLUENCE OF TEMPERATURE ON LYSOZYME CRYSTALS. STRUCTURE AND DYNAMICS OF PROTEIN AND WATER

Structural highlights

1lsd 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 1.7Å
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

Lysozyme structures at six different temperatures in the range 95-295 K have been determined using X-ray crystallography at a resolution of 1.7 A. The crystals at lower temperatures had a 7.4% decrease in the unit-cell volume. The volume change was discontinuous with the volume being near 238 000 A(3) from 295 to 250 K and about 220 200 A(3) below 180 K. The thermal expansion of the protein has been analyzed and shows anisotropy, which is correlated with local atomic packing and secondary-structure elements. The lysozyme structure at low temperature is nearly the same as that at high temperature, with only small relative translations and rotations of structure elements including a hinge-bending rearrangement of two domains. Because of a considerable increase of lattice disorder at low temperature dynamical analysis of internal motion is difficult. The analysis of structural and dynamical properties of well ordered protein-bound water has been carried out.

The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water.,Kurinov IV, Harrison RW Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):98-109. PMID:15299341[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. ↑ Kurinov IV, Harrison RW. The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water. Acta Crystallogr D Biol Crystallogr. 1995 Jan 1;51(Pt 1):98-109. PMID:15299341 doi:http://dx.doi.org/10.1107/S0907444994009261

1lsd, resolution 1.70Å

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