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2job

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Revision as of 08:15, 19 January 2022

Solution structure of an antilipopolysaccharide factor from shrimp and its possible Lipid A binding site

Structural highlights

2job is a 1 chain structure with sequence from Giant tiger prawn. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and (15)N uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C(34)--C(55) disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which prevented us to experimentally determine by NMR the binding mode of these lipids to rALF-Pm3. However, on the basis of striking structural similarities to the FhuA/LPS complex, we designed an original model of the possible lipid A-binding site of ALF-Pm3. Such a binding site, located on the ALF-Pm3 beta-sheet and involving seven charged residues, is well conserved in ALF-L from Limulus polyphemus and in ALF-T from Tachypleus tridentatus. In addition, our model is in agreement with experiments showing that beta-hairpin synthetic peptides corresponding to ALF-L beta-sheet bind to LPS. Delineating lipid A-binding site of ALFs will help go further in the de novo design of new antibacterial or LPS-neutralizing drugs. (c) 2008 Wiley Periodicals, Inc. Biopolymers 91: 207-220, 2009.This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com.

NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site.,Yang Y, Boze H, Chemardin P, Padilla A, Moulin G, Tassanakajon A, Pugniere M, Roquet F, Destoumieux-Garzon D, Gueguen Y, Bachere E, Aumelas A Biopolymers. 2009 Mar;91(3):207-20. PMID:19107926^[1]

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

References

↑ Yang Y, Boze H, Chemardin P, Padilla A, Moulin G, Tassanakajon A, Pugniere M, Roquet F, Destoumieux-Garzon D, Gueguen Y, Bachere E, Aumelas A. NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site. Biopolymers. 2009 Mar;91(3):207-20. PMID:19107926 doi:10.1002/bip.21119

1 Structural highlights
2 Evolutionary Conservation
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/2job"

@@ Line 3: / Line 3: @@
 <StructureSection load='2job' size='340' side='right'caption='[[2job]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2job]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Giant_tiger_prawn Giant tiger prawn]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JOB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2job]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Giant_tiger_prawn Giant tiger prawn]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JOB FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2job FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2job OCA], [http://pdbe.org/2job PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2job RCSB], [http://www.ebi.ac.uk/pdbsum/2job PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2job ProSAT]</span></td></tr>
+</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=2job FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2job OCA], [https://pdbe.org/2job PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2job RCSB], [https://www.ebi.ac.uk/pdbsum/2job PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2job ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2job

From Proteopedia

Revision as of 08:15, 19 January 2022

Solution structure of an antilipopolysaccharide factor from shrimp and its possible Lipid A binding site

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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