1dpw: Difference between revisions

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


{{Structure
==STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD==
|PDB= 1dpw |SIZE=350|CAPTION= <scene name='initialview01'>1dpw</scene>, resolution 1.64&Aring;
<StructureSection load='1dpw' size='340' side='right'caption='[[1dpw]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
<table><tr><td colspan='2'>[[1dpw]] 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=1DPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DPW 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]] 1.64&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=1dpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpw OCA], [https://pdbe.org/1dpw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dpw RCSB], [https://www.ebi.ac.uk/pdbsum/1dpw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dpw ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dpw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dpw OCA], [http://www.ebi.ac.uk/pdbsum/1dpw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dpw 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/dp/1dpw_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=1dpw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hen egg-white lysozyme has been crystallized at slightly alkaline pH using 2-methyl-2,4-pentanediol (MPD) as the precipitant. The crystals are nearly isomorphous to crystals grown at acidic pH using sodium chloride as the precipitant. However, the growth kinetics differ markedly between the two conditions. The major reason for this is a molecule of MPD that binds tightly in between two lysozyme molecules and favors the growth of the crystals along the crystallographic c direction over growth perpendicular to it.


'''STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD'''
Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD.,Weiss MS, Palm GJ, Hilgenfeld R Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):952-8. PMID:10944331<ref>PMID:10944331</ref>


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


==Overview==
==See Also==
Hen egg-white lysozyme has been crystallized at slightly alkaline pH using 2-methyl-2,4-pentanediol (MPD) as the precipitant. The crystals are nearly isomorphous to crystals grown at acidic pH using sodium chloride as the precipitant. However, the growth kinetics differ markedly between the two conditions. The major reason for this is a molecule of MPD that binds tightly in between two lysozyme molecules and favors the growth of the crystals along the crystallographic c direction over growth perpendicular to it.
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
==About this Structure==
<references/>
1DPW 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=1DPW OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD., Weiss MS, Palm GJ, Hilgenfeld R, Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):952-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10944331 10944331]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Hilgenfeld R]]
[[Category: Hilgenfeld, R.]]
[[Category: Palm GJ]]
[[Category: Palm, G J.]]
[[Category: Weiss MS]]
[[Category: Weiss, M S.]]
[[Category: hydrolase]]
[[Category: protein-mpd complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:46:17 2008''

Latest revision as of 02:54, 21 November 2024

STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPDSTRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD

Structural highlights

1dpw 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 1.64Å
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

Hen egg-white lysozyme has been crystallized at slightly alkaline pH using 2-methyl-2,4-pentanediol (MPD) as the precipitant. The crystals are nearly isomorphous to crystals grown at acidic pH using sodium chloride as the precipitant. However, the growth kinetics differ markedly between the two conditions. The major reason for this is a molecule of MPD that binds tightly in between two lysozyme molecules and favors the growth of the crystals along the crystallographic c direction over growth perpendicular to it.

Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD.,Weiss MS, Palm GJ, Hilgenfeld R Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):952-8. PMID:10944331[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. Weiss MS, Palm GJ, Hilgenfeld R. Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD. Acta Crystallogr D Biol Crystallogr. 2000 Aug;56(Pt 8):952-8. PMID:10944331

1dpw, resolution 1.64Å

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