This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2z3m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2z3m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2z3m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2z3m| PDB=2z3m | SCENE= }}
{{STRUCTURE_2z3m| PDB=2z3m | SCENE= }}
-
'''complex structure of LF-transferase and dAF'''
+
===complex structure of LF-transferase and dAF===
-
==Overview==
+
<!--
-
Eubacterial leucyl/phenylalanyl-tRNA protein transferase (LF-transferase) catalyses peptide-bond formation by using Leu-tRNA(Leu) (or Phe-tRNA(Phe)) and an amino-terminal Arg (or Lys) of a protein, as donor and acceptor substrates, respectively. However, the catalytic mechanism of peptide-bond formation by LF-transferase remained obscure. Here we determine the structures of complexes of LF-transferase and phenylalanyl adenosine, with and without a short peptide bearing an N-terminal Arg. Combining the two separate structures into one structure as well as mutation studies reveal the mechanism for peptide-bond formation by LF-transferase. The electron relay from Asp 186 to Gln 188 helps Gln 188 to attract a proton from the alpha-amino group of the N-terminal Arg of the acceptor peptide. This generates the attacking nucleophile for the carbonyl carbon of the aminoacyl bond of the aminoacyl-tRNA, thus facilitating peptide-bond formation. The protein-based mechanism for peptide-bond formation by LF-transferase is similar to the reverse reaction of the acylation step observed in the peptide hydrolysis reaction by serine proteases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17891155}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17891155 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17891155}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Watanabe, K.]]
[[Category: Watanabe, K.]]
[[Category: Lf-transferase]]
[[Category: Lf-transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:55:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:43:31 2008''

Revision as of 23:43, 27 July 2008

Template:STRUCTURE 2z3m

complex structure of LF-transferase and dAF

Template:ABSTRACT PUBMED 17891155

About this Structure

2Z3M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase., Watanabe K, Toh Y, Suto K, Shimizu Y, Oka N, Wada T, Tomita K, Nature. 2007 Oct 18;449(7164):867-71. Epub 2007 Sep 23. PMID:17891155

Page seeded by OCA on Mon Jul 28 02:43:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools