2rng: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2rng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RNG FirstGlance]. <br> | <table><tr><td colspan='2'>[[2rng]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RNG FirstGlance]. <br> | ||
</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=2rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rng OCA], [https://pdbe.org/2rng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rng RCSB], [https://www.ebi.ac.uk/pdbsum/2rng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rng ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</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=2rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rng OCA], [https://pdbe.org/2rng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rng RCSB], [https://www.ebi.ac.uk/pdbsum/2rng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rng ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 11:39, 30 October 2024
Solution structure of big defensinSolution structure of big defensin
Structural highlights
FunctionBDEF_TACTR Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro.[1] Publication Abstract from PubMedBig defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. It has antimicrobial activities against Gram-positive and -negative bacteria. The amino acid sequence of big defensin can be divided into an N-terminal hydrophobic half and a C-terminal cationic half. Interestingly, the trypsin cleaves big defensin into two fragments, the N-terminal and C-terminal fragments, which are responsible for antimicrobial activity against Gram-positive and -negative bacteria, respectively. To explore the antimicrobial mechanism of big defensin, we determined the solution structure of mature big defensin and performed a titration experiment with DPC micelles. Big defensin has a novel defensin structure; the C-terminal domain adopts a beta-defensin structure, and the N-terminal domain forms a unique globular conformation. It is noteworthy that the hydrophobic N-terminal domain undergoes a conformational change in micelle solution, while the C-terminal domain remains unchanged. Here, we propose that the N-terminal domain achieves its antimicrobial activity in a novel fashion and explain that big defensin has developed a strategy different from those of other beta-defensins to suppress the growth of Gram-positive bacteria. A novel beta-defensin structure: a potential strategy of big defensin for overcoming resistance by Gram-positive bacteria.,Kouno T, Fujitani N, Mizuguchi M, Osaki T, Nishimura S, Kawabata S, Aizawa T, Demura M, Nitta K, Kawano K Biochemistry. 2008 Oct 7;47(40):10611-9. Epub 2008 Sep 12. PMID:18785751[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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