1hwp: Difference between revisions

Latest revision as of 08:30, 6 November 2024

EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM

Structural highlights

1hwp is a 2 chain structure with sequence from Sambucus ebulus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Ligands:	BGC, BMA, GAL, NAG, PRD_900004, PT1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9AVR2_SAMEB

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

Ebulin l is a type-II ribosome-inactivating protein (RIP) isolated from the leaves of Sambucus ebulus L. As with other type-II RIP, ebulin is a disulfide-linked heterodimer composed of a toxic A chain and a galactoside-specific lectin B chain. A normal level of ribosome-inactivating N-glycosidase activity, characteristic of the A chain of type-II RIP, has been demonstrated for ebulin l. However, ebulin is considered a nontoxic type-II RIP due to a reduced cytotoxicity on whole cells and animals as compared with other toxic type-II RIP like ricin. The molecular cloning, amino acid sequence, and the crystal structure of ebulin l are presented and compared with ricin. Ebulin l is shown to bind an A-chain substrate analogue, pteroic acid, in the same manner as ricin. The galactoside-binding ability of ebulin l is demonstrated crystallographically with a complex of the B chain with galactose and with lactose. The negligible cytotoxicity of ebulin l is apparently due to a reduced affinity for galactosides. An altered mode of galactoside binding in the 2gamma subdomain of the lectin B chain primarily causes the reduced affinity.

2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l.,Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T Proteins. 2001 May 15;43(3):319-26. PMID:11288182^[1]

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

References

↑ Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T. 2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l. Proteins. 2001 May 15;43(3):319-26. PMID:11288182

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Pascal JM, Day PJ, Monzingo AF, Ernst SR, Robertus JD, Iglesias R, Perez Y, Ferreras JM, Citores L, Girbes T. 2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l. Proteins. 2001 May 15;43(3):319-26. PMID:11288182

[1]

@@ Line 1: / Line 1: @@
 ==EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM==
-<StructureSection load='1hwp' size='340' side='right' caption='[[1hwp]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='1hwp' size='340' side='right'caption='[[1hwp]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hwp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HWP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hwp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sambucus_ebulus Sambucus ebulus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HWP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PT1:PTEROIC+ACID'>PT1</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]] 3.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hwn|1hwn]], [[1hwo|1hwo]], [[1hwm|1hwm]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene>, <scene name='pdbligand=PT1:PTEROIC+ACID'>PT1</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1hwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwp OCA], [https://pdbe.org/1hwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hwp RCSB], [https://www.ebi.ac.uk/pdbsum/1hwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwp ProSAT]</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=1hwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hwp OCA], [http://pdbe.org/1hwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hwp RCSB], [http://www.ebi.ac.uk/pdbsum/1hwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hwp ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q9AVR2_SAMEB Q9AVR2_SAMEB]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hw/1hwp_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Sambucus ebulus]]
-[[Category: RRNA N-glycosylase]]
+[[Category: Day PJ]]
-[[Category: Day, P J]]
+[[Category: Ernst SR]]
-[[Category: Ernst, S R]]
+[[Category: Monzingo AF]]
-[[Category: Monzingo, A F]]
+[[Category: Pascal JM]]
-[[Category: Pascal, J M]]
+[[Category: Robertus JD]]
-[[Category: Robertus, J D]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Ribosome-inactivating protein]]
-[[Category: Ricin-like]]

1hwp: Difference between revisions

Latest revision as of 08:30, 6 November 2024

EBULIN COMPLEXED WITH PTEROIC ACID, TRIGONAL CRYSTAL FORM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

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