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000142547 0247_ $$2pmid$$apmid:23086131
000142547 0247_ $$2doi$$a10.1007/s00018-012-1184-1
000142547 0247_ $$2ISSN$$a1420-9071
000142547 0247_ $$2ISSN$$a0014-4754
000142547 0247_ $$2ISSN$$a1420-682X
000142547 0247_ $$2WOS$$aWOS:000315343600011
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000142547 037__ $$aPHPPUBDB-25506
000142547 041__ $$aEnglish
000142547 082__ $$a570
000142547 1001_ $$aLeysen, S.$$b0
000142547 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000142547 245__ $$aStructural basis of bacterial defense against g-type lysozyme-based innate immunity
000142547 260__ $$aBasel$$bBirkhäuser$$c2013
000142547 300__ $$a1-10
000142547 3367_ $$2DRIVER$$aarticle
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000142547 440_0 $$0PERI:(DE-600)1458497-9$$aCell. Mol. Life Sci.$$v72$$x1420-682X
000142547 500__ $$3Converted on 2013-05-30 09:57$$a© Springer Basel; Post referee fulltext in progress; Embargo 12 months from publication 
000142547 500__ $$3Converted on 2013-06-21 19:21
000142547 520__ $$aGram-negative bacteria can produce specific proteinaceous inhibitors to defend themselves against the lytic action of host lysozymes. So far, four different lysozyme inhibitor families have been identified. Here, we report the crystal structure of the Escherichia coli periplasmic lysozyme inhibitor of g-type lysozyme (PliG-Ec) in complex with Atlantic salmon g-type lysozyme (SalG) at a resolution of 0.95 Å, which is exceptionally high for a complex of two proteins. The structure reveals for the first time the mechanism of g-type lysozyme inhibition by the PliG family. The latter contains two specific conserved regions that are essential for its inhibitory activity. The inhibitory complex formation is based on a double 'key-lock' mechanism. The first key-lock element is formed by the insertion of two conserved PliG regions into the active site of the lysozyme. The second element is defined by a distinct pocket of PliG accommodating a lysozyme loop. Computational analysis indicates that this pocket represents a suitable site for small molecule binding, which opens an avenue for the development of novel antibacterial agents that suppress the inhibitory activity of PliG.
000142547 536__ $$0G:(DE-H253)POF2-D1.2-20130405$$aDORIS Beamline D1.2 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000142547 588__ $$aDataset connected to Pubmed
000142547 650_7 $$00$$2NLM Chemicals$$aEscherichia coli Proteins
000142547 650_7 $$00$$2NLM Chemicals$$aPliG protein, E coli
000142547 650_7 $$0EC 3.2.1.17$$2NLM Chemicals$$aMuramidase
000142547 650_2 $$2MeSH$$aAnimals
000142547 650_2 $$2MeSH$$aCrystallography
000142547 650_2 $$2MeSH$$aEscherichia coli: chemistry
000142547 650_2 $$2MeSH$$aEscherichia coli: immunology
000142547 650_2 $$2MeSH$$aEscherichia coli Proteins: chemistry
000142547 650_2 $$2MeSH$$aEscherichia coli Proteins: metabolism
000142547 650_2 $$2MeSH$$aImmunity, Innate: immunology
000142547 650_2 $$2MeSH$$aModels, Molecular
000142547 650_2 $$2MeSH$$aMuramidase: chemistry
000142547 650_2 $$2MeSH$$aMuramidase: metabolism
000142547 650_2 $$2MeSH$$aProtein Conformation
000142547 650_2 $$2MeSH$$aSalmo salar
000142547 693__ $$0EXP:(DE-H253)D-D1.2-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-D1.2-20150101$$aDORIS III$$fDORIS Beamline D1.2$$x0
000142547 7001_ $$aVanderkelen, L.$$b1
000142547 7001_ $$aWeeks, S. D.$$b2
000142547 7001_ $$aMichiels, C. W.$$b3
000142547 7001_ $$0P:(DE-HGF)0$$aStrelkov, S. V.$$b4$$eCorresponding author
000142547 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-012-1184-1$$gVol. 70, p. 1-10$$p1-10$$q70<1-10$$tCellular and molecular life sciences$$v70$$x1420-682X$$y2013
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000142547 9141_ $$a(c) Springer. COde P.  It's not published yet$$y2013
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