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| | <StructureSection load='4v35' size='340' side='right'caption='[[4v35]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4v35' size='340' side='right'caption='[[4v35]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v35]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V35 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v35]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V35 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v34|4v34]], [[4v36|4v36]]</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=4v35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v35 OCA], [https://pdbe.org/4v35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v35 RCSB], [https://www.ebi.ac.uk/pdbsum/4v35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v35 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanylphosphatidylglycerol_synthase Alanylphosphatidylglycerol synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.11 2.3.2.11] </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=4v35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v35 OCA], [http://pdbe.org/4v35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v35 RCSB], [http://www.ebi.ac.uk/pdbsum/4v35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v35 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9I537_PSEAE Q9I537_PSEAE] |
| | <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: Alanylphosphatidylglycerol synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Hasenkampf, T]] | + | [[Category: Hasenkampf T]] |
| - | [[Category: Hebecker, S]] | + | [[Category: Hebecker S]] |
| - | [[Category: Heinz, D W]] | + | [[Category: Heinz DW]] |
| - | [[Category: Krausze, J]] | + | [[Category: Krausze J]] |
| - | [[Category: Moser, J]] | + | [[Category: Moser J]] |
| - | [[Category: A-pg]]
| + | |
| - | [[Category: Bacterial resistance protein]]
| + | |
| - | [[Category: Lipid homeostasis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trna-dependent aminoacylation]]
| + | |
| Structural highlights
4v35 is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q9I537_PSEAE
Publication Abstract from PubMed
The cytoplasmic membrane is probably the most important physical barrier between microbes and the surrounding habitat. Aminoacylation of the polar head group of the phospholipid phosphatidylglycerol (PG) catalyzed by Ala-tRNAAla-dependent alanyl-phosphatidylglycerol synthase (A-PGS) or by Lys-tRNALys-dependent lysyl-phosphatidylglycerol synthase (L-PGS) enables bacteria to cope with cationic peptides that are harmful to the integrity of the cell membrane. Accordingly, these synthases also have been designated as multiple peptide resistance factors (MprF). They consist of a separable C-terminal catalytic domain and an N-terminal transmembrane flippase domain. Here we present the X-ray crystallographic structure of the catalytic domain of A-PGS from the opportunistic human pathogen Pseudomonas aeruginosa. In parallel, the structure of the related lysyl-phosphatidylglycerol-specific L-PGS domain from Bacillus licheniformis in complex with the substrate analog L-lysine amide is presented. Both proteins reveal a continuous tunnel that allows the hydrophobic lipid substrate PG and the polar aminoacyl-tRNA substrate to access the catalytic site from opposite directions. Substrate recognition of A-PGS versus L-PGS was investigated using misacylated tRNA variants. The structural work presented here in combination with biochemical experiments using artificial tRNA or artificial lipid substrates reveals the tRNA acceptor stem, the aminoacyl moiety, and the polar head group of PG as the main determinants for substrate recognition. A mutagenesis approach yielded the complementary amino acid determinants of tRNA interaction. These results have broad implications for the design of L-PGS and A-PGS inhibitors that could render microbial pathogens more susceptible to antimicrobial compounds.
Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine.,Hebecker S, Krausze J, Hasenkampf T, Schneider J, Groenewold M, Reichelt J, Jahn D, Heinz DW, Moser J Proc Natl Acad Sci U S A. 2015 Aug 10. pii: 201511167. PMID:26261323[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hebecker S, Krausze J, Hasenkampf T, Schneider J, Groenewold M, Reichelt J, Jahn D, Heinz DW, Moser J. Structures of two bacterial resistance factors mediating tRNA-dependent aminoacylation of phosphatidylglycerol with lysine or alanine. Proc Natl Acad Sci U S A. 2015 Aug 10. pii: 201511167. PMID:26261323 doi:http://dx.doi.org/10.1073/pnas.1511167112
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