2cxa

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[[Image:2cxa.gif|left|200px]]
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{{Structure
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|PDB= 2cxa |SIZE=350|CAPTION= <scene name='initialview01'>2cxa</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_2cxa", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_2cxa| PDB=2cxa | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cxa OCA], [http://www.ebi.ac.uk/pdbsum/2cxa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cxa RCSB]</span>
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'''Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli'''
'''Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli'''
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Revision as of 20:16, 3 May 2008

Template:STRUCTURE 2cxa

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


Overview

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.

About this Structure

2CXA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 23:16:33 2008

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