2mvo

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'''Unreleased structure'''
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==Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024==
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<StructureSection load='2mvo' size='340' side='right' caption='[[2mvo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2mvo]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MVO FirstGlance]. <br>
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</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=2mvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mvo RCSB], [http://www.ebi.ac.uk/pdbsum/2mvo PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The investigation of self-resistance in antibiotic producers is important to understand the emergence of antibiotic resistance in pathogens and to improve antibiotic production. Lantibiotics are ribosomally synthesized antibiotics that mostly target peptidoglycan biosynthesis. The actinomycete Microbispora ATCC PTA-5024 produces the lantibiotic NAI-107, which interferes with peptidoglycan biosynthesis by binding bactoprenol-pyrophosphate-coupled peptidoglycan precursors. In order to understand how Microbispora counteracts the action of its own antibiotic, its peptidoglycan composition was analysed in detail. Microbispora peptidoglycan consists of muropeptides with D-Ala and Gly in similar proportion at the fourth position of the peptide stems and alternative 3-3 cross-links besides the classical 4-3 cross-links. In addition, the NAI-107 biosynthetic gene cluster (mlb) was analysed for the expression of immunity proteins. We show that distinct immunity determinants are encoded in the mlb cluster: the ABC transporter MlbYZ acting cooperatively with the transmembrane protein MlbJ and the lipoprotein MlbQ. NMR structural analysis of MlbQ revealed a hydrophobic surface patch, which is proposed to bind the cognate lantibiotic. This study demonstrates that immunity in Microbispora is not only based on one determinant but on the action of the distinct immunity proteins MlbQ, MlbYZ and MlbJ.
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The entry 2mvo is ON HOLD until Paper Publication
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Distinct mechanisms contribute to immunity in the lantibiotic NAI-107 producer strain Microbispora ATCC PTA-5024.,Pozzi R, Coles M, Linke D, Kulik A, Nega M, Wohlleben W, Stegmann E Environ Microbiol. 2015 Apr 29. doi: 10.1111/1462-2920.12892. PMID:25923468<ref>PMID:25923468</ref>
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Authors: Pozzi, R., Schwartz, P., Linke, D., Kulik, A., Nega, M., Wohlleben, W., Stegmann, E., Coles, M.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Coles, M]]
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[[Category: Kulik, A]]
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[[Category: Linke, D]]
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[[Category: Nega, M]]
[[Category: Pozzi, R]]
[[Category: Pozzi, R]]
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[[Category: Wohlleben, W]]
 
[[Category: Schwartz, P]]
[[Category: Schwartz, P]]
[[Category: Stegmann, E]]
[[Category: Stegmann, E]]
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[[Category: Linke, D]]
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[[Category: Wohlleben, W]]
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[[Category: Coles, M]]
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[[Category: Lantibiotic resistance]]
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[[Category: Kulik, A]]
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[[Category: Lipid binding protein]]
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[[Category: Nega, M]]
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[[Category: Lipoprotein]]

Revision as of 13:19, 15 July 2015

Solution structure of the lantibiotic self-resistance lipoprotein MlbQ from Microbispora ATCC PTA-5024

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