|
|
| (14 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| - | [[Image:1kve.gif|left|200px]]<br /><applet load="1kve" size="450" color="white" frame="true" align="right" spinBox="true" | |
| - | caption="1kve, resolution 1.8Å" /> | |
| - | '''KILLER TOXIN FROM HALOTOLERANT YEAST'''<br /> | |
| | | | |
| - | ==Overview== | + | ==KILLER TOXIN FROM HALOTOLERANT YEAST== |
| - | BACKGROUND: Several strains of yeasts and fungi produce proteinous, substances, termed killer toxins, which kill sensitive strains. The SMK, toxin, secreted by the halotolerant yeast Pichia farinosa KK1 strain, uniquely exhibits its maximum killer activity under conditions of acidic, pH and high salt concentration. The toxin is composed of two distinct, subunits, alpha and beta, which tightly interact with each other under, acidic conditions. However, they are easily dissociated under neutral, conditions and lose the killer activity. The three-dimensional structure, of the SMK toxin will provide a better understanding of the mechanism of, toxicity of this protein and the cause of its unique pH-dependent, stability. RESULTS: Two crystal structures of the SMK toxin have been, determined at 1.8 A resolution in different ionic strength conditions. The, two subunits, alpha and beta, are jointly folded into an ellipsoidal, single domain structure belonging to the alpha/beta-sandwich family. The, folding topology of the SMK toxin is essentially the same as that of the, fungal killer toxin, KP4. This shared topology contains two left-handed, split betaalphabeta motifs, which are rare in the other proteins. Many, acidic residues are clustered at the bottom of the SMK toxin molecule., Some of the carboxyl sidechains interact with each other through hydrogen, bonds. The ionic strength difference induces no evident structural change, of the SMK toxin except that, in the high ionic strength crystal, a number, of sulfate ions are electrostatically bound near the basic residues which, are also locally distributed at the bottom of the toxin molecule., CONCLUSIONS: The two killer toxins, SMK and KP4, share a unique folding, topology which contains a rare structural motif. This observation may, suggest that these toxins are evolutionally and/or functionally related., The pH-dependent stability of the SMK toxin is a result of the intensive, interactions between the carboxyl groups. This finding is important for, protein engineering, for instance, towards stabilization of the toxin, molecule in a broader pH range. The present crystallographic study, revealed that the structure of the SMK toxin itself is hardly affected by, the ionic strength, implying that a high salt concentration affects the, sensitivity of the cell against the toxin. | + | <StructureSection load='1kve' size='340' side='right'caption='[[1kve]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[1kve]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Millerozyma_farinosa Millerozyma farinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KVE 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]] 1.8Å</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=1kve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kve OCA], [https://pdbe.org/1kve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kve RCSB], [https://www.ebi.ac.uk/pdbsum/1kve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kve ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TOXK_MILFA TOXK_MILFA] This toxin kills sensitive strains of yeast. |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | BACKGROUND: Several strains of yeasts and fungi produce proteinous substances, termed killer toxins, which kill sensitive strains. The SMK toxin, secreted by the halotolerant yeast Pichia farinosa KK1 strain, uniquely exhibits its maximum killer activity under conditions of acidic pH and high salt concentration. The toxin is composed of two distinct subunits, alpha and beta, which tightly interact with each other under acidic conditions. However, they are easily dissociated under neutral conditions and lose the killer activity. The three-dimensional structure of the SMK toxin will provide a better understanding of the mechanism of toxicity of this protein and the cause of its unique pH-dependent stability. RESULTS: Two crystal structures of the SMK toxin have been determined at 1.8 A resolution in different ionic strength conditions. The two subunits, alpha and beta, are jointly folded into an ellipsoidal, single domain structure belonging to the alpha/beta-sandwich family. The folding topology of the SMK toxin is essentially the same as that of the fungal killer toxin, KP4. This shared topology contains two left-handed split betaalphabeta motifs, which are rare in the other proteins. Many acidic residues are clustered at the bottom of the SMK toxin molecule. Some of the carboxyl sidechains interact with each other through hydrogen bonds. The ionic strength difference induces no evident structural change of the SMK toxin except that, in the high ionic strength crystal, a number of sulfate ions are electrostatically bound near the basic residues which are also locally distributed at the bottom of the toxin molecule. CONCLUSIONS: The two killer toxins, SMK and KP4, share a unique folding topology which contains a rare structural motif. This observation may suggest that these toxins are evolutionally and/or functionally related. The pH-dependent stability of the SMK toxin is a result of the intensive interactions between the carboxyl groups. This finding is important for protein engineering, for instance, towards stabilization of the toxin molecule in a broader pH range. The present crystallographic study revealed that the structure of the SMK toxin itself is hardly affected by the ionic strength, implying that a high salt concentration affects the sensitivity of the cell against the toxin. |
| | | | |
| - | ==About this Structure==
| + | The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin.,Kashiwagi T, Kunishima N, Suzuki C, Tsuchiya F, Nikkuni S, Arata Y, Morikawa K Structure. 1997 Jan 15;5(1):81-94. PMID:9016714<ref>PMID:9016714</ref> |
| - | 1KVE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pichia_farinosa Pichia farinosa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KVE OCA].
| + | |
| | | | |
| - | ==Reference==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin., Kashiwagi T, Kunishima N, Suzuki C, Tsuchiya F, Nikkuni S, Arata Y, Morikawa K, Structure. 1997 Jan 15;5(1):81-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9016714 9016714]
| + | </div> |
| - | [[Category: Pichia farinosa]] | + | <div class="pdbe-citations 1kve" style="background-color:#fffaf0;"></div> |
| - | [[Category: Protein complex]] | + | == References == |
| - | [[Category: Arata, Y.]] | + | <references/> |
| - | [[Category: Kashiwagi, T.]] | + | __TOC__ |
| - | [[Category: Kunishima, N.]] | + | </StructureSection> |
| - | [[Category: Morikawa, K.]] | + | [[Category: Large Structures]] |
| - | [[Category: Nikkuni, S.]] | + | [[Category: Millerozyma farinosa]] |
| - | [[Category: Suzuki, C.]] | + | [[Category: Arata Y]] |
| - | [[Category: Tsuchiya, F.]] | + | [[Category: Kashiwagi T]] |
| - | [[Category: halotolerant yeast]]
| + | [[Category: Kunishima N]] |
| - | [[Category: toxin]]
| + | [[Category: Morikawa K]] |
| - | | + | [[Category: Nikkuni S]] |
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:55:28 2007''
| + | [[Category: Suzuki C]] |
| | + | [[Category: Tsuchiya F]] |
| Structural highlights
Function
TOXK_MILFA This toxin kills sensitive strains of yeast.
Publication Abstract from PubMed
BACKGROUND: Several strains of yeasts and fungi produce proteinous substances, termed killer toxins, which kill sensitive strains. The SMK toxin, secreted by the halotolerant yeast Pichia farinosa KK1 strain, uniquely exhibits its maximum killer activity under conditions of acidic pH and high salt concentration. The toxin is composed of two distinct subunits, alpha and beta, which tightly interact with each other under acidic conditions. However, they are easily dissociated under neutral conditions and lose the killer activity. The three-dimensional structure of the SMK toxin will provide a better understanding of the mechanism of toxicity of this protein and the cause of its unique pH-dependent stability. RESULTS: Two crystal structures of the SMK toxin have been determined at 1.8 A resolution in different ionic strength conditions. The two subunits, alpha and beta, are jointly folded into an ellipsoidal, single domain structure belonging to the alpha/beta-sandwich family. The folding topology of the SMK toxin is essentially the same as that of the fungal killer toxin, KP4. This shared topology contains two left-handed split betaalphabeta motifs, which are rare in the other proteins. Many acidic residues are clustered at the bottom of the SMK toxin molecule. Some of the carboxyl sidechains interact with each other through hydrogen bonds. The ionic strength difference induces no evident structural change of the SMK toxin except that, in the high ionic strength crystal, a number of sulfate ions are electrostatically bound near the basic residues which are also locally distributed at the bottom of the toxin molecule. CONCLUSIONS: The two killer toxins, SMK and KP4, share a unique folding topology which contains a rare structural motif. This observation may suggest that these toxins are evolutionally and/or functionally related. The pH-dependent stability of the SMK toxin is a result of the intensive interactions between the carboxyl groups. This finding is important for protein engineering, for instance, towards stabilization of the toxin molecule in a broader pH range. The present crystallographic study revealed that the structure of the SMK toxin itself is hardly affected by the ionic strength, implying that a high salt concentration affects the sensitivity of the cell against the toxin.
The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin.,Kashiwagi T, Kunishima N, Suzuki C, Tsuchiya F, Nikkuni S, Arata Y, Morikawa K Structure. 1997 Jan 15;5(1):81-94. PMID:9016714[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kashiwagi T, Kunishima N, Suzuki C, Tsuchiya F, Nikkuni S, Arata Y, Morikawa K. The novel acidophilic structure of the killer toxin from halotolerant yeast demonstrates remarkable folding similarity with a fungal killer toxin. Structure. 1997 Jan 15;5(1):81-94. PMID:9016714
|
