4hr6: Difference between revisions
New page: '''Unreleased structure''' The entry 4hr6 is ON HOLD Authors: Sharma, A., Pohlentz, G., Bobbili, K.B., Jeyaprakash, A.A., Chandran, T., Mormann, M., Swamy, M.J., Vijayan, M. Descriptio... |
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The | ==Crystal structure of snake gourd (Trichosanthes anguina) seed lectin, a three chain homologue of type II RIPs== | ||
<StructureSection load='4hr6' size='340' side='right'caption='[[4hr6]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hr6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichosanthes_anguina Trichosanthes anguina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HR6 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]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMG:ALPHA-METHYL-D-GALACTOSIDE'>AMG</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=4hr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hr6 OCA], [https://pdbe.org/4hr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hr6 RCSB], [https://www.ebi.ac.uk/pdbsum/4hr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hr6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/U3KRF6_TRIAN U3KRF6_TRIAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sequence and structure of snake gourd seed lectin (SGSL), a nontoxic homologue of type II ribosome-inactivating proteins (RIPs), have been determined by mass spectrometry and X-ray crystallography, respectively. As in type II RIPs, the molecule consists of a lectin chain made up of two beta-trefoil domains. The catalytic chain, which is connected through a disulfide bridge to the lectin chain in type II RIPs, is cleaved into two in SGSL. However, the integrity of the three-dimensional structure of the catalytic component of the molecule is preserved. This is the first time that a three-chain RIP or RIP homologue has been observed. A thorough examination of the sequence and structure of the protein and of its interactions with the bound methyl-alpha-galactose indicate that the nontoxicity of SGSL results from a combination of changes in the catalytic and the carbohydrate-binding sites. Detailed analyses of the sequences of type II RIPs of known structure and their homologues with unknown structure provide valuable insights into the evolution of this class of proteins. They also indicate some variability in carbohydrate-binding sites, which appears to contribute to the different levels of toxicity exhibited by lectins from various sources. | |||
The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs.,Sharma A, Pohlentz G, Bobbili KB, Jeyaprakash AA, Chandran T, Mormann M, Swamy MJ, Vijayan M Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1493-503. doi:, 10.1107/S0907444913010020. Epub 2013 Jul 18. PMID:23897472<ref>PMID:23897472</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4hr6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Trichosanthes anguina]] | |||
[[Category: Bobbili KB]] | |||
[[Category: Chandran T]] | |||
[[Category: Jeyaprakash AA]] | |||
[[Category: Mormann M]] | |||
[[Category: Pohlentz G]] | |||
[[Category: Sharma A]] | |||
[[Category: Swamy MJ]] | |||
[[Category: Vijayan M]] | |||
Latest revision as of 06:00, 21 November 2024
Crystal structure of snake gourd (Trichosanthes anguina) seed lectin, a three chain homologue of type II RIPsCrystal structure of snake gourd (Trichosanthes anguina) seed lectin, a three chain homologue of type II RIPs
Structural highlights
FunctionPublication Abstract from PubMedThe sequence and structure of snake gourd seed lectin (SGSL), a nontoxic homologue of type II ribosome-inactivating proteins (RIPs), have been determined by mass spectrometry and X-ray crystallography, respectively. As in type II RIPs, the molecule consists of a lectin chain made up of two beta-trefoil domains. The catalytic chain, which is connected through a disulfide bridge to the lectin chain in type II RIPs, is cleaved into two in SGSL. However, the integrity of the three-dimensional structure of the catalytic component of the molecule is preserved. This is the first time that a three-chain RIP or RIP homologue has been observed. A thorough examination of the sequence and structure of the protein and of its interactions with the bound methyl-alpha-galactose indicate that the nontoxicity of SGSL results from a combination of changes in the catalytic and the carbohydrate-binding sites. Detailed analyses of the sequences of type II RIPs of known structure and their homologues with unknown structure provide valuable insights into the evolution of this class of proteins. They also indicate some variability in carbohydrate-binding sites, which appears to contribute to the different levels of toxicity exhibited by lectins from various sources. The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs.,Sharma A, Pohlentz G, Bobbili KB, Jeyaprakash AA, Chandran T, Mormann M, Swamy MJ, Vijayan M Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1493-503. doi:, 10.1107/S0907444913010020. Epub 2013 Jul 18. PMID:23897472[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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