1jjc

From Proteopedia
Revision as of 19:12, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1jjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjc, resolution 2.60Å" /> '''Crystal structure at...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search
File:1jjc.gif


1jjc, resolution 2.60Å

Drag the structure with the mouse to rotate

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

OverviewOverview

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.

About this StructureAbout this Structure

1JJC is a Protein complex structure of sequences from Thermus thermophilus with MN, SO4 and FA5 as ligands. Active as Phenylalanine--tRNA ligase, with EC number 6.1.1.20 Full crystallographic information is available from OCA.

ReferenceReference

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 Nov 20 18:19:20 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA