1b5f: Difference between revisions
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<StructureSection load='1b5f' size='340' side='right'caption='[[1b5f]], [[Resolution|resolution]] 1.72Å' scene=''> | <StructureSection load='1b5f' size='340' side='right'caption='[[1b5f]], [[Resolution|resolution]] 1.72Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b5f]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1b5f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cynara_cardunculus Cynara cardunculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5F FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 1.72Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <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=1b5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5f OCA], [https://pdbe.org/1b5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5f RCSB], [https://www.ebi.ac.uk/pdbsum/1b5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5f ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CARDA_CYNCA CARDA_CYNCA] Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin.[UniProtKB:P85136]<ref>PMID:16428617</ref> <ref>PMID:8654427</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/1b5f_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/1b5f_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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[[Category: Cynara cardunculus]] | [[Category: Cynara cardunculus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bento | [[Category: Bento I]] | ||
[[Category: Carrondo | [[Category: Carrondo MA]] | ||
[[Category: Frazao | [[Category: Frazao C]] | ||
Latest revision as of 09:24, 30 October 2024
NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.
Structural highlights
FunctionCARDA_CYNCA Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin.[UniProtKB:P85136][1] [2] 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 PubMedAspartic proteinases (AP) have been widely studied within the living world, but so far no plant AP have been structurally characterized. The refined cardosin A crystallographic structure includes two molecules, built up by two glycosylated peptide chains (31 and 15 kDa each). The fold of cardosin A is typical within the AP family. The glycosyl content is described by 19 sugar rings attached to Asn-67 and Asn-257. They are localized on the molecular surface away from the conserved active site and show a new glycan of the plant complex type. A hydrogen bond between Gln-126 and Manbeta4 renders the monosaccharide oxygen O-2 sterically inaccessible to accept a xylosyl residue, therefore explaining the new type of the identified plant glycan. The Arg-Gly-Asp sequence, which has been shown to be involved in recognition of a putative cardosin A receptor, was found in a loop between two beta-strands on the molecular surface opposite the active site cleft. Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed. The biological implications of these findings are also discussed. Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L.,Frazao C, Bento I, Costa J, Soares CM, Verissimo P, Faro C, Pires E, Cooper J, Carrondo MA J Biol Chem. 1999 Sep 24;274(39):27694-701. PMID:10488111[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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