1vmo: Difference between revisions

New page: left|200px<br /><applet load="1vmo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vmo, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1vmo.gif|left|200px]]<br /><applet load="1vmo" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY'''<br />


==Overview==
==CRYSTAL STRUCTURE OF VITELLINE MEMBRANE OUTER LAYER PROTEIN I (VMO-I): A FOLDING MOTIF WITH HOMOLOGOUS GREEK KEY STRUCTURES RELATED BY AN INTERNAL THREE-FOLD SYMMETRY==
The crystal structure of vitelline membrane outer layer protein I (VMO-I), which is isolated from the vitelline membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and, refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds, into an unusual structure that consists of three beta-sheets forming Greek, key motifs, which are related by an internal pseudo three-fold symmetry., The internal portion surrounded by these three beta-sheets is filled with, hydrophobic side chains. This conformational feature coincides with three, internal repeats in the sequence. Although a similar fold exists in the, second domain of delta-endotoxin, there are significant structural, differences between the two proteins, with the three-fold symmetry being, most regular in VMO-I.
<StructureSection load='1vmo' size='340' side='right'caption='[[1vmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vmo]] is a 2 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=1VMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VMO 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]] 2.2&#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=1vmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vmo OCA], [https://pdbe.org/1vmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vmo RCSB], [https://www.ebi.ac.uk/pdbsum/1vmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vmo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VMO1_CHICK VMO1_CHICK] Exact function not known, component of the outer membrane of the vitelline layer of the egg. Seems to be able to synthesize N-acetylchito-oligosaccharides (n=14-15) from hexasaccharides of N-acetylglucosamine in a manner similar to the transferase activity of lysozyme.
== 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/vm/1vmo_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=1vmo ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of vitelline membrane outer layer protein I (VMO-I), which is isolated from the vitelline membrane outer layer of hen's eggs, has been determined by the multiple isomorphous replacement method and refined to an R-factor of 18.8% at 2.2 A resolution. The main chain folds into an unusual structure that consists of three beta-sheets forming Greek key motifs, which are related by an internal pseudo three-fold symmetry. The internal portion surrounded by these three beta-sheets is filled with hydrophobic side chains. This conformational feature coincides with three internal repeats in the sequence. Although a similar fold exists in the second domain of delta-endotoxin, there are significant structural differences between the two proteins, with the three-fold symmetry being most regular in VMO-I.


==About this Structure==
Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry.,Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K EMBO J. 1994 Mar 1;13(5):1003-10. PMID:8131734<ref>PMID:8131734</ref>
1VMO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VMO OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of vitelline membrane outer layer protein I (VMO-I): a folding motif with homologous Greek key structures related by an internal three-fold symmetry., Shimizu T, Vassylyev DG, Kido S, Doi Y, Morikawa K, EMBO J. 1994 Mar 1;13(5):1003-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8131734 8131734]
</div>
<div class="pdbe-citations 1vmo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Doi, Y.]]
[[Category: Doi Y]]
[[Category: Kido, S.]]
[[Category: Kido S]]
[[Category: Morikawa, K.]]
[[Category: Morikawa K]]
[[Category: Shimizu, T.]]
[[Category: Shimizu T]]
[[Category: Vassylyev, D.G.]]
[[Category: Vassylyev DG]]
[[Category: membrane protein]]
 
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