1jjc: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1jjc.gif|left|200px]]
{{Seed}}
[[Image:1jjc.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jjc|  PDB=1jjc  |  SCENE=  }}  
{{STRUCTURE_1jjc|  PDB=1jjc  |  SCENE=  }}  


'''Crystal structure at 2.6A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese'''
===Crystal structure at 2.6A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese===




==Overview==
<!--
The crystal structure of phenylalanyl-tRNA synthetase (PheRS) from Thermus thermophilus, a class II aminoacyl-tRNA synthetase, complexed with phenylalanyl-adenylate (Phe-AMP) was determined at 2.6 A resolution. Crystals of native PheRS were soaked in a solution containing phenylalanine and ATP in the presence of Mn(2+) ions. The first step of the aminoacylation reaction proceeds within the crystals, resulting in Phe-AMP formation at the active site. Specific recognition of the phenylalanine portion of the Phe-AMP is achieved by interactions of the phenyl ring of Phe-AMP with two neighbouring residues, Phealpha258 and Phealpha260. No manganese ions were observed within the active site; their role in the formation of the transition state may be assigned to a number of polar residues and water molecules. In the anomalous Fourier difference map, a divalent metal ion was detected at the interface of the alpha- and beta-subunits at a short distance from motif 3 residues participating in the substrate binding. A sulfate ion, which was identified on the protein surface, may mediate the interactions of PheRS with DNA. Visible conformational changes were detected in the active-site area adjacent to the position of the Phe-AMP, compared with the structure of PheRS complexed with a synthetic adenylate analogue (phenylalaninyl-adenylate). Based on the known structures of the substrate-free enzyme and its complexes with various ligands, a general scheme for the phenylalanylation mechanism is proposed.
The line below this paragraph, {{ABSTRACT_PUBMED_11679717}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11679717 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11679717}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Phenylalanyl-trna]]
[[Category: Phenylalanyl-trna]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:17:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:20:01 2008''

Revision as of 17:20, 1 July 2008

File:1jjc.png

Template:STRUCTURE 1jjc

Crystal structure at 2.6A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese

Template:ABSTRACT PUBMED 11679717

About this Structure

1JJC is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese., Fishman R, Ankilova V, Moor N, Safro M, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1534-44. Epub 2001, Oct 25. PMID:11679717

Page seeded by OCA on Tue Jul 1 20:20:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1jjc&oldid=616758"