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Hydrolase PDB-id
1hwp
Asymmetric unit
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Description
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Protein chains
252 a.a. *
263 a.a. *
Ligands
PT1
GAL-BGC
NAG-NAG-BMA
Waters ×20

* Residue conservation analysis
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  Biological unit*, tetramer
(*as deduced by PQS)
PDB id: 1hwp
Name: Hydrolase
Title: Ebulin complexed with pteroic acid, trigonal crystal form

Structure:
Ebulin. Chain: a. Synonym: ebulin a chain. Other_details: n-glycosidase. Ebulin. Chain: b. Synonym: ebulin b chain. Other_details: galactoside specific lectin

Source:
Sambucus ebulus. Organism_taxid: 28503. Tissue: leaf. Tissue: leaf

Biological unit:
Tetramer (from PQS)

UniProt:
Chain A: Q9AVR2 (Q9AVR2_9DIPS)
Pfam   ArchSchema ?
Seq:
Struc:
Seq:
Struc:
Seq: 564 a.a.
Struc: 252 a.a.

Chain B: Q9AVR2 (Q9AVR2_9DIPS)
Pfam   ArchSchema ?
Seq:
Struc:
Seq:
Struc:
Seq: 564 a.a.
Struc: 263 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Enzyme class:
Chains A, B: E.C.3.2.2.22   [IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Reaction:
Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Resolution:
3.10Å

R-factor:
0.219

R-free:
0.317

Authors:
J.M.Pascal,P.J.Day,A.F.Monzingo,S.R.Ernst,J.D.Robertus

Key ref:
J.M.Pascal et al. (2001). 2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l.. Proteins, 43, 319-326. [PubMed id: 11288182] [DOI: 10.1002/prot.1043]

Date:
09-Jan-01

Release date:
24-Jan-01

Related entries:
1hwn
1hwn is ebulin complexed with galactose, trigonal crystal
form
1hwo
1hwo is ebulin complexed with lactose, trigonal crystal for
1hwm
1hwm is ebulin, orthorhombic crystal form, distorted 2gamma
galactoside-binding domain
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    Key reference    
 
 
DOI no: 10.1002/prot.1043 Proteins 43:319-326 (2001)
PubMed id: 11288182  
 
 
2.8-A crystal structure of a nontoxic type-II ribosome-inactivating protein, ebulin l.
J.M.Pascal, P.J.Day, A.F.Monzingo, S.R.Ernst, J.D.Robertus, R.Iglesias, Y.Pérez, J.M.Férreras, L.Citores, T.Girbés.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
Figure 2.
Figure 2. Section of the 2.8-Å electron density for the trigonal model. A 2Fo-Fc map with sigmaA-weighted phases. The map is contoured at 1.3 .
Figure 7.
Figure 7. Comparison of the galactoside-binding, 2 subdomains of ebulin (top) and ricin (bottom). Galactose is bound to ebulin. Lactose is bound to ricin. In both pictures, the galactose moiety is numbered at significant carbons of the sugar ring. All contacts with lactose in ricin are made with the galactose moiety. The glucose moiety (GLC) extends into the solvent. The GLC extension ( -1,4 linkage) from the C1 hydroxyl of the galactose moiety in ricin is not possible for the C1 hydroxyl of galactose in ebulin, because of steric interference with 254 N.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2001, 43, 319-326) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19292877 H.Hemmi, A.Kuno, S.Ito, R.Suzuki, T.Hasegawa, and J.Hirabayashi (2009).
NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.
  FEBS J, 276, 2095-2105.  
18798567 L.Maveyraud, H.Niwa, V.Guillet, D.I.Svergun, P.V.Konarev, R.A.Palmer, W.J.Peumans, P.Rougé, E.J.Van Damme, C.D.Reynolds, and L.Mourey (2009).
Structural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigra.
  Proteins, 75, 89.
PDB codes: 3c9z 3ca0 3ca1 3ca3 3ca4 3ca5 3ca6 3cah
19056784 M.L.DeMarco, and R.J.Woods (2009).
Atomic-resolution conformational analysis of the GM3 ganglioside in a lipid bilayer and its implications for ganglioside-protein recognition at membrane surfaces.
  Glycobiology, 19, 344-355.  
16772301 A.Bagaria, K.Surendranath, U.A.Ramagopal, S.Ramakumar, and A.A.Karande (2006).
Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin.
  J Biol Chem, 281, 34465-34474.
PDB code: 2amz
16122386 B.Pils, R.R.Copley, and J.Schultz (2005).
Variation in structural location and amino acid conservation of functional sites in protein domain families.
  BMC Bioinformatics, 6, 210.  
15774467 V.Mishra, S.Bilgrami, R.S.Sharma, P.Kaur, S.Yadav, R.Krauspenhaar, C.Betzel, W.Voelter, C.R.Babu, and T.P.Singh (2005).
Crystal structure of himalayan mistletoe ribosome-inactivating protein reveals the presence of a natural inhibitor and a new functionally active sugar-binding site.
  J Biol Chem, 280, 20712-20721.
PDB code: 1yf8
14686924 A.Chambery, A.Di Maro, M.M.Monti, F.Stirpe, and A.Parente (2004).
Volkensin from Adenia volkensii Harms (kilyambiti plant), a type 2 ribosome-inactivating protein.
  Eur J Biochem, 271, 108-117.  
15388944 R.Suzuki, Z.Fujimoto, A.Kuno, J.Hirabayashi, K.Kasai, and T.Hasegawa (2004).
Crystallization and preliminary X-ray crystallographic studies of the C-terminal domain of galactose-binding lectin EW29 from the earthworm Lumbricus terrestris.
  Acta Crystallogr D Biol Crystallogr, 60, 1895-1896.  
15194688 T.Uchida, T.Yamasaki, S.Eto, H.Sugawara, G.Kurisu, A.Nakagawa, M.Kusunoki, and T.Hatakeyama (2004).
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism.
  J Biol Chem, 279, 37133-37141.
PDB code: 1vcl
15583377 V.Mishra, A.S.Ethayathulla, R.S.Sharma, S.Yadav, R.Krauspenhaar, C.Betzel, C.R.Babu, and T.P.Singh (2004).
Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas.
  Acta Crystallogr D Biol Crystallogr, 60, 2295-2304.
PDB code: 1pc8
12611897 J.Morlon-Guyot, M.Helmy, S.Lombard-Frasca, D.Pignol, G.Piéroni, and B.Beaumelle (2003).
Identification of the ricin lipase site and implication in cytotoxicity.
  J Biol Chem, 278, 17006-17011.  
11836254 R.P.Kruger, H.C.Winter, N.Simonson-Leff, J.A.Stuckey, I.J.Goldstein, and J.E.Dixon (2002).
Cloning, expression, and characterization of the Galalpha 1,3Gal high affinity lectin from the mushroom Marasmius oreades.
  J Biol Chem, 277, 15002-15005.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.