5e5q: Difference between revisions
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<table><tr><td colspan='2'>[[5e5q]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E5Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e5q]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E5Q FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e5t|5e5t]], [[5e5y|5e5y]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5e5t|5e5t]], [[5e5y|5e5y]]</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=5e5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5q OCA], [http://pdbe.org/5e5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5q RCSB], [http://www.ebi.ac.uk/pdbsum/5e5q PDBsum]</span></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=5e5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e5q OCA], [http://pdbe.org/5e5q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e5q RCSB], [http://www.ebi.ac.uk/pdbsum/5e5q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e5q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 09:18, 26 July 2016
Racemic snakin-1 in P21/cRacemic snakin-1 in P21/c
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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