2cxa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2cxa.gif|left|200px]]<br /><applet load="2cxa" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2cxa.gif|left|200px]]
-
caption="2cxa, resolution 1.60&Aring;" />
+
 
-
'''Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli'''<br />
+
{{Structure
 +
|PDB= 2cxa |SIZE=350|CAPTION= <scene name='initialview01'>2cxa</scene>, resolution 1.60&Aring;
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY= [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]
 +
|GENE=
 +
}}
 +
 
 +
'''Crystal structure of Leucyl/phenylalanyl-tRNA protein transferase from Escherichia coli'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
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].
+
2CXA is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242373 17242373]
+
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://www.ncbi.nlm.nih.gov/pubmed/17242373 17242373]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Leucyltransferase]]
[[Category: Leucyltransferase]]
Line 20: Line 29:
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: aminoacyl-trna]]
[[Category: aminoacyl-trna]]
-
[[Category: national project on protein structural and functional analyses]]
+
[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: nppsfa]]
[[Category: protein degradation]]
[[Category: protein degradation]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
-
[[Category: structural genomics]]
+
[[Category: structural genomic]]
[[Category: transferase]]
[[Category: transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:19 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:20:53 2008''

Revision as of 14:20, 20 March 2008


PDB ID 2cxa

Drag the structure with the mouse to rotate
, resolution 1.60Å
Activity: Leucyltransferase, with EC number 2.3.2.6
Coordinates: save as pdb, mmCIF, xml



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 Thu Mar 20 16:20:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools