1viw: Difference between revisions

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[[Image:1viw.gif|left|200px]]
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{{STRUCTURE_1viw|  PDB=1viw  |  SCENE=  }}
'''TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX'''


==TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX==
<StructureSection load='1viw' size='340' side='right'caption='[[1viw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1viw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] and [https://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIW 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1viw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1viw OCA], [https://pdbe.org/1viw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1viw RCSB], [https://www.ebi.ac.uk/pdbsum/1viw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1viw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LEA1_PHAVU LEA1_PHAVU] Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects.[:]
== 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/vi/1viw_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=1viw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The alpha-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the alpha-amylase inhibitor (alpha-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic alpha-amylase (PPA) and alpha-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to alpha-amylases, large deviations from the mammalian alpha-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian alpha-amylase.


==Overview==
A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor.,Nahoum V, Farisei F, Le-Berre-Anton V, Egloff MP, Rouge P, Poerio E, Payan F Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):360-2. Epub 1999, Jan 1. PMID:10089450<ref>PMID:10089450</ref>
The alpha-amylase from Tenebrio molitor larvae (TMA) has been crystallized in complex with the alpha-amylase inhibitor (alpha-AI) from the bean Phaseolus vulgaris. A molecular-replacement solution of the structure was obtained using the refined pig pancreatic alpha-amylase (PPA) and alpha-AI atomic coordinates as starting models. The structural analysis showed that although TMA has the typical structure common to alpha-amylases, large deviations from the mammalian alpha-amylase models occur in the loops. Despite these differences in the interacting loops, the bean inhibitor is still able to inhibit both the insect and mammalian alpha-amylase.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1VIW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris] and [http://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIW OCA].
</div>
<div class="pdbe-citations 1viw" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A plant-seed inhibitor of two classes of alpha-amylases: X-ray analysis of Tenebrio molitor larvae alpha-amylase in complex with the bean Phaseolus vulgaris inhibitor., Nahoum V, Farisei F, Le-Berre-Anton V, Egloff MP, Rouge P, Poerio E, Payan F, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):360-2. Epub 1999, Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089450 10089450]
*[[Amylase 3D structures|Amylase 3D structures]]
[[Category: Alpha-amylase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phaseolus vulgaris]]
[[Category: Phaseolus vulgaris]]
[[Category: Protein complex]]
[[Category: Tenebrio molitor]]
[[Category: Tenebrio molitor]]
[[Category: Egloff, M P.]]
[[Category: Egloff MP]]
[[Category: Nahoum, V.]]
[[Category: Nahoum V]]
[[Category: Payan, F.]]
[[Category: Payan F]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Insect alpha-amylase]]
[[Category: Lectin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon May 26 22:54:27 2008''

Latest revision as of 07:33, 30 October 2024

TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX

1viw, resolution 3.00Å

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