1b5f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b5f, resolution 1.72&Aring;" /> '''NATIVE CARDOSIN A FR...)
Current revision (06:24, 30 October 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1b5f.gif|left|200px]]<br /><applet load="1b5f" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1b5f, resolution 1.72&Aring;" />
 
-
'''NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.'''<br />
 
-
==Overview==
+
==NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.==
-
Aspartic 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.
+
<StructureSection load='1b5f' size='340' side='right'caption='[[1b5f]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
 +
<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>
 +
== 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 ==
 +
[[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/b5/1b5f_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=1b5f ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Aspartic 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.
-
==About this Structure==
+
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<ref>PMID:10488111</ref>
-
1B5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cynara_cardunculus Cynara cardunculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B5F OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10488111 10488111]
+
</div>
 +
<div class="pdbe-citations 1b5f" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Cynara cardunculus]]
[[Category: Cynara cardunculus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Bento, I.]]
+
[[Category: Bento I]]
-
[[Category: Carrondo, M.A.]]
+
[[Category: Carrondo MA]]
-
[[Category: Frazao, C.]]
+
[[Category: Frazao C]]
-
[[Category: hydrolase(aspartic proteinase)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:44:49 2007''
+

Current revision

NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.

PDB ID 1b5f

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b5f"
Personal tools