3o5w

From Proteopedia

(Difference between revisions)

Current revision

Binding of kinetin in the active site of mistletoe lectin I

Structural highlights

3o5w is a 2 chain structure with sequence from Viscum album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ML1_VISAL The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The crystal structure of the ribosome inhibiting protein Mistletoe Lectin I (ML-I) derived from the European mistletoe, Viscum album, in complex with kinetin has been refined at 2.7A resolution. Suitably large crystals of ML-I were obtained applying the counter diffusion method using the Gel Tube R Crystallization Kit (GT-R) on board the Russian Service Module on the international space station ISS within the GCF mission No. 6, arranged by the Japanese aerospace exploration agency (JAXA). Hexagonal bi-pyramidal crystals were grown during three months under microgravity. Before data collection the crystals were soaked in a saturated solution of kinetin and diffraction data to 2.7A were collected using synchrotron radiation and cryogenic techniques. The atomic model was refined and revealed a single kinetin molecule in the ribosome inactivation site of ML-I. The complex demonstrates the feasibility of mistletoe to bind plant hormones out of the host regulation system as part of a self protection mechanism.

Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album.,Malecki PH, Rypniewski W, Szymanski M, Barciszewski J, Meyer A Biochim Biophys Acta. 2012 Feb;1824(2):334-8. doi: 10.1016/j.bbapap.2011.10.013. , Epub 2011 Oct 28. PMID:22064121^[4]

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

References

↑ Kourmanova AG, Soudarkina OJ, Olsnes S, Kozlov JV. Cloning and characterization of the genes encoding toxic lectins in mistletoe (Viscum album L). Eur J Biochem. 2004 Jun;271(12):2350-60. PMID:15182350 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04153.x
↑ Mishra V, Sharma RS, Yadav S, Babu CR, Singh TP. Purification and characterization of four isoforms of Himalayan mistletoe ribosome-inactivating protein from Viscum album having unique sugar affinity. Arch Biochem Biophys. 2004 Mar 15;423(2):288-301. PMID:15001393 doi:http://dx.doi.org/10.1016/j.abb.2003.12.033
↑ Dietrich JB, Ribereau-Gayon G, Jung ML, Franz H, Beck JP, Anton R. Identity of the N-terminal sequences of the three A chains of mistletoe (Viscum album L.) lectins: homology with ricin-like plant toxins and single-chain ribosome-inhibiting proteins. Anticancer Drugs. 1992 Oct;3(5):507-11. PMID:1450445
↑ Malecki PH, Rypniewski W, Szymanski M, Barciszewski J, Meyer A. Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album. Biochim Biophys Acta. 2012 Feb;1824(2):334-8. doi: 10.1016/j.bbapap.2011.10.013. , Epub 2011 Oct 28. PMID:22064121 doi:http://dx.doi.org/10.1016/j.bbapap.2011.10.013

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3o5w"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3o5w is ON HOLD  until Paper Publication
+==Binding of kinetin in the active site of mistletoe lectin I==
+<StructureSection load='3o5w' size='340' side='right'caption='[[3o5w]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3o5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5W 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]] 2.7&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H35:N-(FURAN-2-YLMETHYL)-7H-PURIN-6-AMINE'>H35</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3o5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5w OCA], [https://pdbe.org/3o5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5w RCSB], [https://www.ebi.ac.uk/pdbsum/3o5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5w ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ML1_VISAL ML1_VISAL] The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.<ref>PMID:15182350</ref> <ref>PMID:15001393</ref> <ref>PMID:1450445</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the ribosome inhibiting protein Mistletoe Lectin I (ML-I) derived from the European mistletoe, Viscum album, in complex with kinetin has been refined at 2.7A resolution. Suitably large crystals of ML-I were obtained applying the counter diffusion method using the Gel Tube R Crystallization Kit (GT-R) on board the Russian Service Module on the international space station ISS within the GCF mission No. 6, arranged by the Japanese aerospace exploration agency (JAXA). Hexagonal bi-pyramidal crystals were grown during three months under microgravity. Before data collection the crystals were soaked in a saturated solution of kinetin and diffraction data to 2.7A were collected using synchrotron radiation and cryogenic techniques. The atomic model was refined and revealed a single kinetin molecule in the ribosome inactivation site of ML-I. The complex demonstrates the feasibility of mistletoe to bind plant hormones out of the host regulation system as part of a self protection mechanism.
-Authors: Malecki, P.H., Meyer, A., Rypniewski, W., Szymanski, M., Barciszewski, J., Betzel, C.
+Binding of the plant hormone kinetin in the active site of Mistletoe Lectin I from Viscum album.,Malecki PH, Rypniewski W, Szymanski M, Barciszewski J, Meyer A Biochim Biophys Acta. 2012 Feb;1824(2):334-8. doi: 10.1016/j.bbapap.2011.10.013. , Epub 2011 Oct 28. PMID:22064121<ref>PMID:22064121</ref>
-Description: Binding of kinetin in the active site of mistletoe lectin I
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 29 07:55:29 2010''
+<div class="pdbe-citations 3o5w" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Viscum album]]
+[[Category: Barciszewski J]]
+[[Category: Betzel C]]
+[[Category: Malecki PH]]
+[[Category: Meyer A]]
+[[Category: Rypniewski W]]
+[[Category: Szymanski M]]

3o5w

From Proteopedia

Current revision

Binding of kinetin in the active site of mistletoe lectin I

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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