3a57

From Proteopedia

(Difference between revisions)

Revision as of 16:17, 22 December 2021

Crystal structure of Thermostable Direct Hemolysin

Structural highlights

3a57 is a 1 chain structure with sequence from "oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	tdh ("Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HLY2_VIBPA] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.

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

Thermostable direct hemolysin (TDH) is a major virulence factor of Vibrio parahaemolyticus that causes pandemic foodborne enterocolitis mediated by seafood. TDH exists as a tetramer in solution, and it possesses extreme hemolytic activity. Here, we present the crystal structure of the TDH tetramer at 1.5 A resolution. The TDH tetramer forms a central pore with dimensions of 23 A in diameter and approximately 50 A in depth. Pi-cation interactions between protomers comprising the tetramer were indispensable for hemolytic activity of TDH. The N-terminal region was intrinsically disordered outside of the pore. Molecular dynamic simulations suggested that water molecules permeate freely through the central and side channel pores. Electron micrographs showed that tetrameric TDH attached to liposomes, and some of the tetramer associated with liposome via one protomer. These findings imply a novel membrane attachment mechanism by a soluble tetrameric pore-forming toxin.

Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin.,Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H J Biol Chem. 2010 May 21;285(21):16267-74. Epub 2010 Mar 24. PMID:20335168^[1]

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

References

↑ Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H. Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. J Biol Chem. 2010 May 21;285(21):16267-74. Epub 2010 Mar 24. PMID:20335168 doi:10.1074/jbc.M109.074526

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a57"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Thermostable Direct Hemolysin==
-<StructureSection load='3a57' size='340' side='right' caption='[[3a57]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='3a57' size='340' side='right'caption='[[3a57]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a57]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A57 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"oceanomonas_parahaemolytica"_(fujino_et_al._1951)_miyamoto_et_al._1961 "oceanomonas parahaemolytica" (fujino et al. 1951) miyamoto et al. 1961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A57 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tdh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=670 "Oceanomonas parahaemolytica" (Fujino et al. 1951) Miyamoto et al. 1961])</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=3a57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a57 OCA], [http://pdbe.org/3a57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a57 RCSB], [http://www.ebi.ac.uk/pdbsum/3a57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a57 ProSAT]</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=3a57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a57 OCA], [https://pdbe.org/3a57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a57 RCSB], [https://www.ebi.ac.uk/pdbsum/3a57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a57 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HLY2_VIBPA HLY2_VIBPA]] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.
+[[https://www.uniprot.org/uniprot/HLY2_VIBPA HLY2_VIBPA]] Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by mechanisms not clearly defined.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Hemolysin|Hemolysin]]
+*[[Hemolysin 3D structures|Hemolysin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Fukui, T]]
 [[Category: Hamada, D]]

3a57

From Proteopedia

Revision as of 16:17, 22 December 2021

Crystal structure of Thermostable Direct Hemolysin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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