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<StructureSection load='3u4x' size='340' side='right'caption='[[3u4x]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='3u4x' size='340' side='right'caption='[[3u4x]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Camptosema_pedicellatum Camptosema pedicellatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U4X FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u4x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bionia_pedicellata Bionia pedicellata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U4X FirstGlance]. <br>
</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XMM:(2R,3S,4S,5S,6R)-2-(5-BROMO-4-CHLORO-1H-INDOL-3-YLOXY)-TETRAHYDRO-6-(HYDROXYMETHYL)-2H-PYRAN-3,4,5-TRIOL'>XMM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=XMM:(2R,3S,4S,5S,6R)-2-(5-BROMO-4-CHLORO-1H-INDOL-3-YLOXY)-TETRAHYDRO-6-(HYDROXYMETHYL)-2H-PYRAN-3,4,5-TRIOL'>XMM</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=3u4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4x OCA], [https://pdbe.org/3u4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u4x RCSB], [https://www.ebi.ac.uk/pdbsum/3u4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4x ProSAT]</span></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=3u4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u4x OCA], [https://pdbe.org/3u4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u4x RCSB], [https://www.ebi.ac.uk/pdbsum/3u4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u4x ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/LECA_BIOPE LECA_BIOPE]
Lectins have been used as models for studies of the molecular basis of protein-carbohydrate interaction and specificity by deciphering codes present in the glycan structures. The purpose of the present study was to purify and solve the complete primary and crystal structure of the lectin of Camptosema pedicellatum (CPL) complexed with 5-bromo-4-chloro-3-indolyl-alpha-d-mannose (X-Man) using tandem mass spectrometry. CPL was purified by single-step affinity chromatography. Mass spectrometry findings revealed that purified CPL features a combination of chains weighing 25,298 +/- 2 (alpha-chain), 12,835 +/- 2 (beta-chain) and 12,481 +/- 2 Da (gamma-chain). The solved crystal structure of CPL features a conservative mutation in the hydrophobic subsite, a constituent of the carbohydrate recognition domain (CRD), indicating the relevance of hydrophobic interactions in the establishment of interactions with carbohydrates. The substitution and the analysis of the interactions with X-Man also revealed that the hydrophobic effect caused by a minor change in the hydrophobic subsite interferes in the formation of H-bonds due to the reorientation of the indolyl group in the CRD.
 
Crystal structure of the lectin of Camptosema pedicellatum: implications of a conservative substitution at the hydrophobic subsite.,Souza Teixeira C, da Silva HC, de Moura TR, Pereira-Junior FN, do Nascimento KS, Nagano CS, Sampaio AH, Delatorre P, Rocha BA, Cavada BS J Biochem. 2012 Jul;152(1):87-98. Epub 2012 May 2. PMID:22554687<ref>PMID:22554687</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3u4x" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Camptosema pedicellatum]]
[[Category: Bionia pedicellata]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cavada, B S]]
[[Category: Cavada BS]]
[[Category: Delatorre, P]]
[[Category: Delatorre P]]
[[Category: Moura, T R]]
[[Category: Moura TR]]
[[Category: Nagano, C S]]
[[Category: Nagano CS]]
[[Category: Pereira-Junior, F N]]
[[Category: Pereira-Junior FN]]
[[Category: Rocha, B A.M]]
[[Category: Rocha BAM]]
[[Category: Silva, H C]]
[[Category: Silva HC]]
[[Category: Teixeira, C S]]
[[Category: Teixeira CS]]
[[Category: Carbohydrate-binding protein]]
[[Category: Jelly-roll domain]]
[[Category: Lectin]]

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