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[[Image:1nio.gif|left|200px]]


{{Structure
==Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution==
|PDB= 1nio |SIZE=350|CAPTION= <scene name='initialview01'>1nio</scene>, resolution 2.00&Aring;
<StructureSection load='1nio' size='340' side='right'caption='[[1nio]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
<table><tr><td colspan='2'>[[1nio]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Luffa_aegyptiaca Luffa aegyptiaca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NIO FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22]  
</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&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1nio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nio OCA], [https://pdbe.org/1nio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nio RCSB], [https://www.ebi.ac.uk/pdbsum/1nio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nio ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution'''
== Function ==
 
[https://www.uniprot.org/uniprot/RIPB_LUFAE RIPB_LUFAE]  
 
== Evolutionary Conservation ==
==Overview==
[[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/ni/1nio_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=1nio ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.
The crystal structure of beta-luffin at 2.0 A resolution was solved by the molecular-replacement method using polyalanyl trichosanthin as the search model. The structure was refined with CNS1.1, giving R(work) = 0.162 and R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are 0.008 A and 1.3 degrees, respectively. The overall structure is similar to those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are linked to residues Asn2, Asn78 and Asn85 of the protein.


==About this Structure==
Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution.,Ma QJ, Li JH, Li HG, Wu S, Dong YC Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. Epub 2003, Jul 23. PMID:12876337<ref>PMID:12876337</ref>
1NIO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Luffa_aegyptiaca Luffa aegyptiaca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIO OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution., Ma QJ, Li JH, Li HG, Wu S, Dong YC, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. Epub 2003, Jul 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12876337 12876337]
</div>
<div class="pdbe-citations 1nio" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Luffa aegyptiaca]]
[[Category: Luffa aegyptiaca]]
[[Category: Single protein]]
[[Category: Wu S]]
[[Category: rRNA N-glycosylase]]
[[Category: Wu, S.]]
[[Category: NAG]]
[[Category: beta-luffin]]
[[Category: crystal structure]]
[[Category: ribosome inactivating protein(rip)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:28 2008''

Latest revision as of 07:04, 30 October 2024

Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

1nio, resolution 2.00Å

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