1nli: Difference between revisions

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==Complex of [E160A-E189A] trichosanthin and adenine==
==Complex of [E160A-E189A] trichosanthin and adenine==
<StructureSection load='1nli' size='340' side='right' caption='[[1nli]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='1nli' size='340' side='right'caption='[[1nli]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nli]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_cucumber Chinese cucumber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NLI FirstGlance]. <br>
<table><tr><td colspan='2'>[[1nli]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chinese_cucumber Chinese cucumber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NLI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trichosanthin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3677 Chinese cucumber])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trichosanthin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3677 Chinese cucumber])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nli OCA], [http://pdbe.org/1nli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nli RCSB], [http://www.ebi.ac.uk/pdbsum/1nli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nli ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nli OCA], [http://pdbe.org/1nli PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nli RCSB], [http://www.ebi.ac.uk/pdbsum/1nli PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nli ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nli_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nli_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 35: Line 35:
</StructureSection>
</StructureSection>
[[Category: Chinese cucumber]]
[[Category: Chinese cucumber]]
[[Category: Large Structures]]
[[Category: RRNA N-glycosylase]]
[[Category: RRNA N-glycosylase]]
[[Category: Chan, D S.B]]
[[Category: Chan, D S.B]]

Revision as of 11:52, 2 December 2020

Complex of [E160A-E189A] trichosanthin and adenineComplex of [E160A-E189A] trichosanthin and adenine

Structural highlights

1nli is a 1 chain structure with sequence from Chinese cucumber. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:Trichosanthin (Chinese cucumber)
Activity:rRNA N-glycosylase, with EC number 3.2.2.22
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RIPT_TRIKI] Inactivates eukaryotic 60S ribosomal subunits.

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

Trichosanthin is a ribosome-inactivating protein that cleaves specifically the N-glycosidic bond of A-4324 of 28S rRNA. Trichosanthin and its variant [E160A-E189A]-trichosanthin were found to bind an adenine base with a K(d) value of approximately 0.2mM. To determine how this doubly mutated variant of trichosanthin interacts with adenine, the co-crystal structure of [E160A-E189A]-trichosanthin and adenine was resolved to 0.193nm which revealed that the active site conformation of the doubly mutated variant is isomorphous to wild-type trichosanthin. Water molecules were found at locations corresponding to the eliminated side chain of Glu-160 and Glu-189. On the other hand, the adenine base interacted with [E160A-E189A]-trichosanthin in a manner similar to that in wild-type trichosanthin. Our structural analysis illustrates that Glu-160 and Glu-189 in trichosanthin do not play an important role in maintaining the active site conformation and binding adenine, an essential step for substrate-enzyme interaction. On the other hand, removal of two glutamate residues changed a large patch of negatively charged surface to a positive charge, which may account for the destabilization of the oxocarbenium-like transition-state and the significant decrease in ribosome-inactivating activity in [E160A-E189A]-trichosanthin.

Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine.,Shaw PC, Wong KB, Chan DS, Williams RL Toxicon. 2003 Apr;41(5):575-81. PMID:12676436[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Shaw PC, Wong KB, Chan DS, Williams RL. Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine. Toxicon. 2003 Apr;41(5):575-81. PMID:12676436

1nli, resolution 1.93Å

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OCA