3e7r: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:3e7r.png|left|200px]]
-<!--
+==X-ray Crystal Structure of Racemic Plectasin==
-The line below this paragraph, containing "STRUCTURE_3e7r", creates the "Structure Box" on the page.
+<StructureSection load='3e7r' size='340' side='right'caption='[[3e7r]], [[Resolution|resolution]] 1.00&Aring;' 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'>[[3e7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoplectania_nigrella Pseudoplectania nigrella]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E7R 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">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</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=3e7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e7r OCA], [https://pdbe.org/3e7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e7r RCSB], [https://www.ebi.ac.uk/pdbsum/3e7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e7r ProSAT]</span></td></tr>
-{{STRUCTURE_3e7r|  PDB=3e7r  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DEFPL_PSENR DEFPL_PSENR] Antimicrobial peptide that potently acts against several species of Gram-positive bacteria (PubMed:16222292, PubMed:19472324). It selectively inhibits peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20508130). It does not disrupt cell membranes (PubMed:20508130). Is especially active against numerous clinical isolates of S.pneumoniae, including all 90 different serotypes and isolates resistant to clinically used antibiotics (PubMed:16222292). In vitro, shows considerable selectivity for bacteria over mammalian cells (PubMed:16222292). The peptide synthesized in D-amino acids does not show antibacterial activity (PubMed:19472324). In vitro, acts on voltage-gated potassium channels by moderately inhibiting mammalian Kv1.3/KCNA3 (IC(50)=2.8 uM), and moderately inhibiting others potassium channels (PubMed:25568977).<ref>PMID:16222292</ref> <ref>PMID:25568977</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers L-plectasin and D-plectasin were prepared by total chemical synthesis; interestingly, L-plectasin showed the expected antimicrobial activity, while D-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group P1 with one L-plectasin molecule and one D-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%-15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation.
-===X-ray Crystal Structure of Racemic Plectasin===
+Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods.,Mandal K, Pentelute BL, Tereshko V, Thammavongsa V, Schneewind O, Kossiakoff AA, Kent SB Protein Sci. 2009 Jun;18(6):1146-54. PMID:19472324<ref>PMID:19472324</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_19472324}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3e7r" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19472324 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19472324}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3e7r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E7R OCA].
+[[Category: Pseudoplectania nigrella]]
+[[Category: Kent SBH]]
-==Reference==
+[[Category: Kossiakoff AA]]
-<ref group="xtra">PMID:019472324</ref><references group="xtra"/>
+[[Category: Mandal K]]
-[[Category: Kent, S B.H.]]
+[[Category: Pentelute BL]]
-[[Category: Kossiakoff, A A.]]
+[[Category: Tereshko V]]
-[[Category: Mandal, K.]]
-[[Category: Pentelute, B L.]]
-[[Category: Tereshko, V.]]
-[[Category: Antibiotic]]
-[[Category: Antimicrobial]]
-[[Category: Antimicrobial protein]]
-[[Category: Cleavage on pair of basic residue]]
-[[Category: Defensin]]
-[[Category: Plectasin]]
-[[Category: Racemic protein crystallography]]
-[[Category: Secreted]]