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- | [[Image:1ne9.jpg|left|200px]] | |
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- | {{Structure
| + | ==Crystal Structure of Weissella viridescens FemX at 1.7 Ang Resolution== |
- | |PDB= 1ne9 |SIZE=350|CAPTION= <scene name='initialview01'>1ne9</scene>, resolution 1.70Å
| + | <StructureSection load='1ne9' size='340' side='right'caption='[[1ne9]], [[Resolution|resolution]] 1.70Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
| + | <table><tr><td colspan='2'>[[1ne9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NE9 FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | |GENE= femx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1629 Weissella viridescens])
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ne9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ne9 OCA], [https://pdbe.org/1ne9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ne9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ne9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ne9 ProSAT]</span></td></tr> |
- | |RELATEDENTRY= | + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ne9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ne9 OCA], [http://www.ebi.ac.uk/pdbsum/1ne9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ne9 RCSB]</span>
| + | == Function == |
- | }}
| + | [https://www.uniprot.org/uniprot/FEMX_WEIVI FEMX_WEIVI] Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism (PubMed:11083873, PubMed:4248527, PubMed:12679335, PubMed:15901708, PubMed:23744707). Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide (PubMed:15901708). Also acts on L-seryl-tRNA(Ser) (PubMed:4248527).<ref>PMID:11083873</ref> <ref>PMID:12679335</ref> <ref>PMID:15901708</ref> <ref>PMID:23744707</ref> <ref>PMID:4248527</ref> |
- | | + | == Evolutionary Conservation == |
- | '''Crystal Structure of Weissella viridescens FemX at 1.7 Ang Resolution'''
| + | [[Image:Consurf_key_small.gif|200px|right]] |
- | | + | Check<jmol> |
- | | + | <jmolCheckbox> |
- | ==Overview== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1ne9_consurf.spt"</scriptWhenChecked> |
- | Members of the FemABX protein family are novel therapeutic targets, as they are involved in the synthesis of the bacterial cell wall. They catalyze the addition of amino acid(s) on the peptidoglycan precursor using aminoacylated tRNA as a substrate. We report here the high-resolution structure of Weissella viridescens L-alanine transferase FemX and its complex with the UDP-MurNAc-pentapeptide. This is the first structure example of a FemABX family member that does not possess a coiled-coil domain. FemX consists of two structurally equivalent domains, separated by a cleft containing the binding site of the UDP-MurNAc-pentapeptide and a long channel that traverses one of the two domains. Our structural studies bring new insights into the evolution of the FemABX and the related GNAT superfamilies, shed light on the recognition site of the aminoacylated tRNA in Fem proteins, and allowed manual docking of the acceptor end of the alanyl-tRNAAla.
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | | + | <text>to colour the structure by Evolutionary Conservation</text> |
- | ==About this Structure== | + | </jmolCheckbox> |
- | 1NE9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Weissella_viridescens Weissella viridescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NE9 OCA].
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ne9 ConSurf]. |
- | | + | <div style="clear:both"></div> |
- | ==Reference== | + | == References == |
- | Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: insights into FemABX family substrates recognition., Biarrotte-Sorin S, Maillard AP, Delettre J, Sougakoff W, Arthur M, Mayer C, Structure. 2004 Feb;12(2):257-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14962386 14962386]
| + | <references/> |
- | [[Category: Single protein]] | + | __TOC__ |
| + | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Weissella viridescens]] | | [[Category: Weissella viridescens]] |
- | [[Category: Arthur, M.]] | + | [[Category: Arthur M]] |
- | [[Category: Biarrotte-Sorin, S.]] | + | [[Category: Biarrotte-Sorin S]] |
- | [[Category: Delettre, J.]] | + | [[Category: Delettre J]] |
- | [[Category: Maillard, A P.]] | + | [[Category: Maillard AP]] |
- | [[Category: Mayer, C.]] | + | [[Category: Mayer C]] |
- | [[Category: Sougakoff, W.]] | + | [[Category: Sougakoff W]] |
- | [[Category: protein]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:29:10 2008''
| + | |
| Structural highlights
Function
FEMX_WEIVI Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism (PubMed:11083873, PubMed:4248527, PubMed:12679335, PubMed:15901708, PubMed:23744707). Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide (PubMed:15901708). Also acts on L-seryl-tRNA(Ser) (PubMed:4248527).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Hegde SS, Shrader TE. FemABX family members are novel nonribosomal peptidyltransferases and important pathogen-specific drug targets. J Biol Chem. 2001 Mar 9;276(10):6998-7003. Epub 2000 Nov 16. PMID:11083873 doi:http://dx.doi.org/10.1074/jbc.M008591200
- ↑ Hegde SS, Blanchard JS. Kinetic and mechanistic characterization of recombinant Lactobacillus viridescens FemX (UDP-N-acetylmuramoyl pentapeptide-lysine N6-alanyltransferase). J Biol Chem. 2003 Jun 20;278(25):22861-7. doi: 10.1074/jbc.M301565200. Epub 2003 , Apr 4. PMID:12679335 doi:http://dx.doi.org/10.1074/jbc.M301565200
- ↑ Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M. Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens. J Bacteriol. 2005 Jun;187(11):3833-8. PMID:15901708 doi:http://dx.doi.org/187/11/3833
- ↑ Fonvielle M, Li de La Sierra-Gallay I, El-Sagheer AH, Lecerf M, Patin D, Mellal D, Mayer C, Blanot D, Gale N, Brown T, van Tilbeurgh H, Etheve-Quelquejeu M, Arthur M. The Structure of FemX in Complex with a Peptidyl-RNA Conjugate: Mechanism of Aminoacyl Transfer from Ala-tRNA to Peptidoglycan Precursors. Angew Chem Int Ed Engl. 2013 Jun 6. doi: 10.1002/anie.201301411. PMID:23744707 doi:10.1002/anie.201301411
- ↑ Plapp R, Strominger JL. Biosynthesis of the peptidoglycan of bacterial cell walls. 18. Purification and properties of L-alanyl transfer ribonucleic acid-uridine diphosphate-N-acetylmuramyl-pentapeptide transferase from Lactobacillus viridescens. J Biol Chem. 1970 Jul 25;245(14):3675-82. PMID:4248527
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