5aa4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of MltF from Pseudomonas aeruginosa in complex with cell-wall tetrapeptide== | |
| + | <StructureSection load='5aa4' size='340' side='right' caption='[[5aa4]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5aa4]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6X4:(2~{R})-5-[[6-AZANYL-1-[[(2~{R})-1-AZANYL-1-OXIDANYLIDENE-PROPAN-2-YL]AMINO]-1-OXIDANYLIDENE-HEXAN-2-YL]AMINO]-5-OXIDANYLIDENE-2-[[(2~{S})-2-[[(2~{R})-2-OXIDANYLPROPANOYL]AMINO]PROPANOYL]AMINO]PENTANOIC+ACID'>6X4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aa1|5aa1]], [[5aa2|5aa2]], [[5aa3|5aa3]]</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=5aa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa4 OCA], [http://pdbe.org/5aa4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa4 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteria grow and divide without loss of cellular integrity. This accomplishment is notable, as a key component of their cell envelope is a surrounding glycopeptide polymer. In Gram-negative bacteria this polymer-the peptidoglycan-grows by the difference between concurrent synthesis and degradation. The regulation of the enzymatic ensemble for these activities is poorly understood. We report herein the structural basis for the control of one such enzyme, the lytic transglycosylase MltF of Pseudomonas aeruginosa. Its structure comprises two modules: an ABC-transporter-like regulatory module and a catalytic module. Occupancy of the regulatory module by peptidoglycan-derived muropeptides effects a dramatic and long-distance (40 A) conformational change, occurring over the entire protein structure, to open its active site for catalysis. This discovery of the molecular basis for the allosteric control of MltF catalysis is foundational to further study of MltF within the complex enzymatic orchestration of the dynamic peptidoglycan. | ||
| - | + | Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa.,Dominguez-Gil T, Lee M, Acebron-Avalos I, Mahasenan KV, Hesek D, Dik DA, Byun B, Lastochkin E, Fisher JF, Mobashery S, Hermoso JA Structure. 2016 Oct 4;24(10):1729-1741. doi: 10.1016/j.str.2016.07.019. Epub 2016, Sep 8. PMID:27618662<ref>PMID:27618662</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5aa4" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Acebron, I]] | [[Category: Acebron, I]] | ||
| + | [[Category: Dominguez-Gil, T]] | ||
| + | [[Category: Hermoso, J A]] | ||
| + | [[Category: Cell wall recycling]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Lytic transglycosilase]] | ||
Revision as of 17:36, 19 October 2016
Crystal structure of MltF from Pseudomonas aeruginosa in complex with cell-wall tetrapeptide
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