1bhz: Difference between revisions

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{{Seed}}
[[Image:1bhz.png|left|200px]]


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==LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA==
The line below this paragraph, containing "STRUCTURE_1bhz", creates the "Structure Box" on the page.
<StructureSection load='1bhz' size='340' side='right'caption='[[1bhz]], [[Resolution|resolution]] 3.90&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'>[[1bhz]] 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=1BHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHZ 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]] 3.9&#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=1bhz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhz OCA], [https://pdbe.org/1bhz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhz RCSB], [https://www.ebi.ac.uk/pdbsum/1bhz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhz ProSAT]</span></td></tr>
{{STRUCTURE_1bhz|  PDB=1bhz  |  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/bh/1bhz_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=1bhz ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A previous article [Fourme et al. (1995). J. Synchrotron Rad. 2, 36-48] presented the theoretical foundations of MASC, a new contrast-variation method using multiwavelength anomalous scattering, and reported the first experimental results. New experiments have been conducted both at the ESRF (Grenoble, France) and at LURE-DCI (Orsay, France), using cryocooled crystals of three proteins of known structures and very different molecular weights. Amplitudes of {GammaT(h)}, the 'normal' structure factors of the anomalously scattering part of the crystal including the solvent zone and the ordered anomalous scattering sites (if any), have been extracted from multiwavelength data. In the very low resolution range (d &gt;/= 20 A), the agreement between experimental {GammaT(h)} and model values calculated from the bulk solvent is all the more satisfactory since the molecular weight of the protein is high. For spacings between 10 and 20 A, the agreement between experimental {GammaT(h)} and model values is also satisfactory if one takes into account ordered anomalous scatterer sites. Such sites have been found in the three cases.


===LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE LYSOZYME FROM MASC DATA===
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values.,Ramin M, Shepard W, Fourme R, Kahn R Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:10089406<ref>PMID:10089406</ref>


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


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_10089406}}, adds the Publication Abstract to the page
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 10089406 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_10089406}}
__TOC__
 
</StructureSection>
==About this Structure==
1BHZ 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=1BHZ OCA].
 
==Reference==
Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values., Ramin M, Shepard W, Fourme R, Kahn R, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):157-67. Epub 1999, Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089406 10089406]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Fourme R]]
[[Category: Fourme, R.]]
[[Category: Kahn R]]
[[Category: Kahn, R.]]
[[Category: Ramin M]]
[[Category: Ramin, M.]]
[[Category: Shepard W]]
[[Category: Shepard, W.]]
[[Category: Hydrolase]]
[[Category: Masc]]
[[Category: Multiwavelength anomalous solvent contrast]]
[[Category: O-glycosyl]]
 
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Retrieved from "https://proteopedia.org/1bhz"