5e5q: Difference between revisions
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==Racemic snakin-1 in P21/c== | |||
<StructureSection load='5e5q' size='340' side='right'caption='[[5e5q]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5e5q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E5Q 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]] 1.6Å</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=5e5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5q OCA], [https://pdbe.org/5e5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e5q RCSB], [https://www.ebi.ac.uk/pdbsum/5e5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5q ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SNAK1_SOLTU SNAK1_SOLTU] Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria.<ref>PMID:9885189</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proteins from the GASA/snakin superfamily are common in plant proteomes and have diverse functions, including hormonal crosstalk, development, and defense. One 63-residue member of this family, snakin-1, an antimicrobial protein from potatoes, has previously been chemically synthesized in a fully active form. Herein the 1.5 A structure of snakin-1, determined by a novel combination of racemic protein crystallization and radiation-damage-induced phasing (RIP), is reported. Racemic crystals of snakin-1 and quasi-racemic crystals incorporating an unnatural 4-iodophenylalanine residue were prepared from chemically synthesized d- and l-proteins. Breakage of the C-I bonds in the quasi-racemic crystals facilitated structure determination by RIP. The crystal structure reveals a unique protein fold with six disulfide crosslinks, presenting a distinct electrostatic surface that may target the protein to microbial cell surfaces. | |||
Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily.,Yeung H, Squire CJ, Yosaatmadja Y, Panjikar S, Lopez G, Molina A, Baker EN, Harris PW, Brimble MA Angew Chem Int Ed Engl. 2016 May 4. doi: 10.1002/anie.201602719. PMID:27145301<ref>PMID:27145301</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5e5q" style="background-color:#fffaf0;"></div> | ||
[[Category: Brimble | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Solanum tuberosum]] | ||
[[Category: Baker EN]] | |||
[[Category: Brimble MA]] | |||
[[Category: Harris PWR]] | |||
[[Category: Panjikar S]] | |||
[[Category: Squire CJ]] | |||
[[Category: Yeung H]] | |||
[[Category: Yosaatmadja Y]] | |||
Latest revision as of 09:13, 5 July 2023
Racemic snakin-1 in P21/cRacemic snakin-1 in P21/c
Structural highlights
FunctionSNAK1_SOLTU Has an antimicrobial activity. Causes a rapid aggregation of both Gram-positive and Gram-negative bacteria, but the antimicrobial activity is not correlated with the capacity to aggregate bacteria.[1] Publication Abstract from PubMedProteins from the GASA/snakin superfamily are common in plant proteomes and have diverse functions, including hormonal crosstalk, development, and defense. One 63-residue member of this family, snakin-1, an antimicrobial protein from potatoes, has previously been chemically synthesized in a fully active form. Herein the 1.5 A structure of snakin-1, determined by a novel combination of racemic protein crystallization and radiation-damage-induced phasing (RIP), is reported. Racemic crystals of snakin-1 and quasi-racemic crystals incorporating an unnatural 4-iodophenylalanine residue were prepared from chemically synthesized d- and l-proteins. Breakage of the C-I bonds in the quasi-racemic crystals facilitated structure determination by RIP. The crystal structure reveals a unique protein fold with six disulfide crosslinks, presenting a distinct electrostatic surface that may target the protein to microbial cell surfaces. Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily.,Yeung H, Squire CJ, Yosaatmadja Y, Panjikar S, Lopez G, Molina A, Baker EN, Harris PW, Brimble MA Angew Chem Int Ed Engl. 2016 May 4. doi: 10.1002/anie.201602719. PMID:27145301[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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