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| | ==Crystal structure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide.== | | ==Crystal structure of MltF from Pseudomonas aeruginosa in complex with NAM-pentapeptide.== |
| - | <StructureSection load='5aa2' size='340' side='right' caption='[[5aa2]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='5aa2' size='340' side='right'caption='[[5aa2]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5aa2]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5aa2]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_BWHPSA013 Pseudomonas aeruginosa BWHPSA013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AA2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AH0:2-(2-ACETYLAMINO-4-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCT-3-YLOXY)-PROPIONIC+ACID'>AH0</scene>, <scene name='pdbligand=API:2,6-DIAMINOPIMELIC+ACID'>API</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AH0:2-(2-ACETYLAMINO-4-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCT-3-YLOXY)-PROPIONIC+ACID'>AH0</scene>, <scene name='pdbligand=API:2,6-DIAMINOPIMELIC+ACID'>API</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aa1|5aa1]], [[5aa3|5aa3]], [[5aa4|5aa4]]</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=5aa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa2 OCA], [https://pdbe.org/5aa2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aa2 RCSB], [https://www.ebi.ac.uk/pdbsum/5aa2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa2 ProSAT]</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=5aa2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa2 OCA], [http://pdbe.org/5aa2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa2 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MLTF_PSEAE MLTF_PSEAE]] Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.[HAMAP-Rule:MF_02016] | + | [https://www.uniprot.org/uniprot/MLTF_PSEAE MLTF_PSEAE] Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.[HAMAP-Rule:MF_02016] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudomonas aeruginosa]] | + | [[Category: Large Structures]] |
| - | [[Category: Acebron, I]] | + | [[Category: Pseudomonas aeruginosa BWHPSA013]] |
| - | [[Category: Dominguez-Gil, T]] | + | [[Category: Acebron I]] |
| - | [[Category: Hermoso, J A]] | + | [[Category: Dominguez-Gil T]] |
| - | [[Category: Cell wall recycling]]
| + | [[Category: Hermoso JA]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Lytic transglycosilase]]
| + | |
| Structural highlights
5aa2 is a 5 chain structure with sequence from Pseudomonas aeruginosa BWHPSA013. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.8Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
MLTF_PSEAE Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.[HAMAP-Rule:MF_02016]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dominguez-Gil T, Lee M, Acebron-Avalos I, Mahasenan KV, Hesek D, Dik DA, Byun B, Lastochkin E, Fisher JF, Mobashery S, Hermoso JA. Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa. Structure. 2016 Oct 4;24(10):1729-1741. doi: 10.1016/j.str.2016.07.019. Epub 2016, Sep 8. PMID:27618662 doi:http://dx.doi.org/10.1016/j.str.2016.07.019
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