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[[Image:1bwh.png|left|200px]]


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==THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME==
The line below this paragraph, containing "STRUCTURE_1bwh", creates the "Structure Box" on the page.
<StructureSection load='1bwh' size='340' side='right'caption='[[1bwh]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1bwh]] 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=1BWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWH FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwh OCA], [https://pdbe.org/1bwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwh RCSB], [https://www.ebi.ac.uk/pdbsum/1bwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwh ProSAT]</span></td></tr>
{{STRUCTURE_1bwh|  PDB=1bwh  |  SCENE=  }}
</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/bw/1bwh_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=1bwh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.


===THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME===
Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution.,Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:10089304<ref>PMID:10089304</ref>


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


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_10089304}}, adds the Publication Abstract to the page
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10089304 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_10089304}}
__TOC__
 
</StructureSection>
==About this Structure==
1BWH is a 1 chain 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=1BWH OCA].
 
==Reference==
<ref group="xtra">PMID:10089304</ref><references group="xtra"/>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Bi, R C.]]
[[Category: Bi RC]]
[[Category: Boggon, T J.]]
[[Category: Boggon TJ]]
[[Category: Chayen, N E.]]
[[Category: Chayen NE]]
[[Category: Dong, J.]]
[[Category: Dong J]]
[[Category: Raftery, J.]]
[[Category: Raftery J]]
[[Category: 4-beta-n-acetylmuramidase c]]
[[Category: Lysozyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 11:25:12 2009''

Latest revision as of 08:44, 9 August 2023

THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG WHITE LYSOZYMETHE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME

Structural highlights

1bwh 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 1.8Å
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

A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.

Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution.,Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:10089304[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. ↑ Dong J, Boggon TJ, Chayen NE, Raftery J, Bi RC, Helliwell JR. Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):745-52. PMID:10089304

1bwh, resolution 1.80Å

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