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2cxa

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[[Image:2cxa.gif|left|200px]]<br /><applet load="2cxa" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2cxa, resolution 1.60&Aring;" />
 
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'''Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli'''<br />
 
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==Overview==
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==Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli==
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Leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) is an N-end, rule pathway enzyme, which catalyzes the transfer of Leu and Phe from, aminoacyl-tRNAs to exposed N-terminal Arg or Lys residues of acceptor, proteins. Here, we report the 1.6 A resolution crystal structure of, L/F-transferase (JW0868) from Escherichia coli, the first, three-dimensional structure of an L/F-transferase. The L/F-transferase, adopts a monomeric structure consisting of two domains that form a, bilobate molecule. The N-terminal domain forms a small lobe with a novel, fold. The large C-terminal domain has a highly conserved fold, which is, observed in the GCN5-related N-acetyltransferase (GNAT) family. Most of, the conserved residues of L/F-transferase reside in the central cavity, which exists at the interface between the N-terminal and C-terminal, domains. A comparison of the structures of L/F-transferase and the, bacterial peptidoglycan synthase FemX, indicated a structural homology in, the C-terminal domain, and a similar domain interface region. Although the, peptidyltransferase function is shared between the two proteins, the, enzymatic mechanism would differ. The conserved residues in the central, cavity of L/F-transferase suggest that this region is important for the, enzyme catalysis.
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<StructureSection load='2cxa' size='340' side='right'caption='[[2cxa]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cxa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CXA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cxa OCA], [https://pdbe.org/2cxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cxa RCSB], [https://www.ebi.ac.uk/pdbsum/2cxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cxa ProSAT], [https://www.topsan.org/Proteins/RSGI/2cxa TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LFTR_ECOLI LFTR_ECOLI] Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cx/2cxa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2cxa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) is an N-end rule pathway enzyme, which catalyzes the transfer of Leu and Phe from aminoacyl-tRNAs to exposed N-terminal Arg or Lys residues of acceptor proteins. Here, we report the 1.6 A resolution crystal structure of L/F-transferase (JW0868) from Escherichia coli, the first three-dimensional structure of an L/F-transferase. The L/F-transferase adopts a monomeric structure consisting of two domains that form a bilobate molecule. The N-terminal domain forms a small lobe with a novel fold. The large C-terminal domain has a highly conserved fold, which is observed in the GCN5-related N-acetyltransferase (GNAT) family. Most of the conserved residues of L/F-transferase reside in the central cavity, which exists at the interface between the N-terminal and C-terminal domains. A comparison of the structures of L/F-transferase and the bacterial peptidoglycan synthase FemX, indicated a structural homology in the C-terminal domain, and a similar domain interface region. Although the peptidyltransferase function is shared between the two proteins, the enzymatic mechanism would differ. The conserved residues in the central cavity of L/F-transferase suggest that this region is important for the enzyme catalysis.
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==About this Structure==
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The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli.,Dong X, Kato-Murayama M, Muramatsu T, Mori H, Shirouzu M, Bessho Y, Yokoyama S Protein Sci. 2007 Mar;16(3):528-34. Epub 2007 Jan 22. PMID:17242373<ref>PMID:17242373</ref>
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2CXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Leucyltransferase Leucyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.6 2.3.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CXA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli., Dong X, Kato-Murayama M, Muramatsu T, Mori H, Shirouzu M, Bessho Y, Yokoyama S, Protein Sci. 2007 Mar;16(3):528-34. Epub 2007 Jan 22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242373 17242373]
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</div>
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<div class="pdbe-citations 2cxa" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Leucyltransferase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Bessho Y]]
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[[Category: Bessho, Y.]]
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[[Category: Kato-Murayama M]]
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[[Category: Kato-Murayama, M.]]
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[[Category: Shirouzu M]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Yokoyama S]]
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[[Category: Shirouzu, M.]]
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[[Category: Yokoyama, S.]]
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[[Category: aminoacyl-trna]]
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[[Category: national project on protein structural and functional analyses]]
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[[Category: nppsfa]]
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[[Category: protein degradation]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:23:31 2008''
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Current revision

Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli

PDB ID 2cxa

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