View source for 1xe4


==Crystal Structure of Weissella viridescens FemX (K36M) Mutant==
<StructureSection load='1xe4' size='340' side='right'caption='[[1xe4]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xe4]] 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=1XE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XE4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xe4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xe4 OCA], [https://pdbe.org/1xe4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xe4 RCSB], [https://www.ebi.ac.uk/pdbsum/1xe4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xe4 ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xe/1xe4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1xe4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Weissella viridescens FemX (FemX(Wv)) belongs to the Fem family of nonribosomal peptidyl transferases that use aminoacyl-tRNA as the amino acid donor to synthesize the peptide cross-bridge found in the peptidoglycan of many species of pathogenic gram-positive bacteria. We have recently solved the crystal structure of FemX(Wv) in complex with the peptidoglycan precursor UDP-MurNAc-pentapeptide and report here the site-directed mutagenesis of nine residues located in the binding cavity for this substrate. Two substitutions, Lys36Met and Arg211Met, depressed FemX(Wv) transferase activity below detectable levels without affecting protein folding. Analogues of UDP-MurNAc-pentapeptide lacking the phosphate groups or the C-terminal D-alanyl residues were not substrates of the enzyme. These results indicate that Lys36 and Arg211 participate in a complex hydrogen bond network that connects the C-terminal D-Ala residues to the phosphate groups of UDP-MurNAc-pentapeptide and constrains the substrate in a conformation that is essential for transferase activity.

Structure-based site-directed mutagenesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens.,Maillard AP, Biarrotte-Sorin S, Villet R, Mesnage S, Bouhss A, Sougakoff W, Mayer C, Arthur M J Bacteriol. 2005 Jun;187(11):3833-8. PMID:15901708<ref>PMID:15901708</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xe4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Weissella viridescens]]
[[Category: Arthur M]]
[[Category: Biarrotte-Sorin S]]
[[Category: Maillard AP]]
[[Category: Mayer C]]