2ojm: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2ojm.png|left|200px]]


<!--
==Solution structure and cell selectivity of Piscidin 1 and its analogues==
The line below this paragraph, containing "STRUCTURE_2ojm", creates the "Structure Box" on the page.
<StructureSection load='2ojm' size='340' side='right'caption='[[2ojm]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2ojm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Morone_saxatilis Morone saxatilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OJM FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ojm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ojm OCA], [https://pdbe.org/2ojm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ojm RCSB], [https://www.ebi.ac.uk/pdbsum/2ojm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ojm ProSAT]</span></td></tr>
{{STRUCTURE_2ojm|  PDB=2ojm  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/MORO_MORSA MORO_MORSA] Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.<ref>PMID:11713517</ref> <ref>PMID:17253775</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Piscidin 1 (Pis-1) is a novel cytotoxic peptide with a cationic alpha-helical structure that was isolated from the mast cells of hybrid striped bass [Silphaduang, U., and Noga, E. J. (2001) Nature 414, 268-269]. Pis-1 is not selective for bacterial versus mammalian cells. In the present study, to develop novel antibiotic peptides with selectivity for bacterial cells, we examined the effect of substituting two glycine residues, Gly8 and Gly13, with Ala or Pro on this peptide's structure and biological activities. The bacterial cell selectivity of the peptides decreased in the following order: Gly--&gt;Pro analogues &gt; Gly--&gt;Pro/Ala analogues &gt; Pis-1 &gt; Gly--&gt;Ala analogues. The antimicrobial and hemolytic activities and abilities to permeabilize the model phospholipid membranes were higher for Pis-1 with Gly or Pro at position 8 than for its counterparts with either Gly or Pro at position 13. We determined the tertiary structure of Pis-1 and its analogues in the presence of SDS micelles by NMR spectroscopy. We found that Pis-1 has an alpha-helical structure from Phe2 to Thr21. Also, Pis-1 AA (Gly8, Gly13--&gt;Ala8, Ala13) with higher antibacterial and hemolytic activity than Pis-1 has a stable alpha-helical structure from Phe2 to Thr21. Pis-1 PG (Gly--&gt;Pro8) with bacterial cell selectivity has a hinge structure at Pro8, which provides flexibility in piscidin, followed by a three-turn helix from Val10 to Gly22 in the C-terminal region. Taken together, our results demonstrate that the conformational flexibility provided by introduction of a Pro at position 8, coupled with the primary anchoring of phenylalanines and histidines in the N-terminus to the cell membrane and the optimal length of the C-terminal amphipathic alpha-helix, are the critical factors that confer antibacterial activity and bacterial cell selectivity to Pis-1 PG. Pis-1 PG may be a good candidate for the development of a new drug with potent antibacterial activity but without cytotoxicity.


===Solution structure and cell selectivity of Piscidin 1 and its analogues===
Solution structure and cell selectivity of piscidin 1 and its analogues.,Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:17328560<ref>PMID:17328560</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_17328560}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2ojm" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 17328560 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_17328560}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2OJM is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OJM OCA].
[[Category: Morone saxatilis]]
 
[[Category: Kim Y]]
==Reference==
[[Category: Kim YK]]
Solution structure and cell selectivity of piscidin 1 and its analogues., Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y, Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17328560 17328560]
[[Category: Lee SA]]
[[Category: Single protein]]
[[Category: Kim, Y.]]
[[Category: Kim, Y K.]]
[[Category: Lee, S A.]]
[[Category: Antimicrobial peptide]]
[[Category: Antimicrobial protein]]
[[Category: Membrane]]
[[Category: Piscidin 1]]
[[Category: Proline]]
[[Category: Structure]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:10:51 2008''

Latest revision as of 15:53, 20 December 2023

Solution structure and cell selectivity of Piscidin 1 and its analoguesSolution structure and cell selectivity of Piscidin 1 and its analogues

Structural highlights

2ojm is a 1 chain structure with sequence from Morone saxatilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MORO_MORSA Exhibits broad spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria as well as against a variety of fungi. Has hemolytic activity. Seems to disrupt the membranes by adopting an alpha helical conformation and forming toroidal pores.[1] [2]

Publication Abstract from PubMed

Piscidin 1 (Pis-1) is a novel cytotoxic peptide with a cationic alpha-helical structure that was isolated from the mast cells of hybrid striped bass [Silphaduang, U., and Noga, E. J. (2001) Nature 414, 268-269]. Pis-1 is not selective for bacterial versus mammalian cells. In the present study, to develop novel antibiotic peptides with selectivity for bacterial cells, we examined the effect of substituting two glycine residues, Gly8 and Gly13, with Ala or Pro on this peptide's structure and biological activities. The bacterial cell selectivity of the peptides decreased in the following order: Gly-->Pro analogues > Gly-->Pro/Ala analogues > Pis-1 > Gly-->Ala analogues. The antimicrobial and hemolytic activities and abilities to permeabilize the model phospholipid membranes were higher for Pis-1 with Gly or Pro at position 8 than for its counterparts with either Gly or Pro at position 13. We determined the tertiary structure of Pis-1 and its analogues in the presence of SDS micelles by NMR spectroscopy. We found that Pis-1 has an alpha-helical structure from Phe2 to Thr21. Also, Pis-1 AA (Gly8, Gly13-->Ala8, Ala13) with higher antibacterial and hemolytic activity than Pis-1 has a stable alpha-helical structure from Phe2 to Thr21. Pis-1 PG (Gly-->Pro8) with bacterial cell selectivity has a hinge structure at Pro8, which provides flexibility in piscidin, followed by a three-turn helix from Val10 to Gly22 in the C-terminal region. Taken together, our results demonstrate that the conformational flexibility provided by introduction of a Pro at position 8, coupled with the primary anchoring of phenylalanines and histidines in the N-terminus to the cell membrane and the optimal length of the C-terminal amphipathic alpha-helix, are the critical factors that confer antibacterial activity and bacterial cell selectivity to Pis-1 PG. Pis-1 PG may be a good candidate for the development of a new drug with potent antibacterial activity but without cytotoxicity.

Solution structure and cell selectivity of piscidin 1 and its analogues.,Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:17328560[3]

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

References

  1. ↑ Silphaduang U, Noga EJ. Peptide antibiotics in mast cells of fish. Nature. 2001 Nov 15;414(6861):268-9. PMID:11713517 doi:http://dx.doi.org/10.1038/35104690
  2. ↑ Campagna S, Saint N, Molle G, Aumelas A. Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry. 2007 Feb 20;46(7):1771-8. Epub 2007 Jan 25. PMID:17253775 doi:10.1021/bi0620297
  3. ↑ Lee SA, Kim YK, Lim SS, Zhu WL, Ko H, Shin SY, Hahm KS, Kim Y. Solution structure and cell selectivity of piscidin 1 and its analogues. Biochemistry. 2007 Mar 27;46(12):3653-63. Epub 2007 Mar 1. PMID:17328560 doi:10.1021/bi062233u
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2ojm&oldid=4002478"