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Categories: Escherichia coli | Methionine--tRNA ligase | Single protein | Blanquet, S. | Konno, M. | Maveyraud, L. | Mechulam, Y. | Nureki, O. | Schmitt, E. | Yokoyama, S. | Zelwer, C. | ZN | Helix bundle | Rossmann fold | Trna ligase
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1qqt

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(New page: 200px<br /><applet load="1qqt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqt, resolution 2.03&Aring;" /> '''METHIONYL-TRNA SYNTH...)
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Revision as of 22:46, 20 November 2007


1qqt, resolution 2.03Å

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METHIONYL-TRNA SYNTHETASE FROM ESCHERICHIA COLI

Overview

The 3D structure of monomeric C-truncated Escherichia coli methionyl-tRNA, synthetase, a class 1 aminoacyl-tRNA synthetase, has been solved at 2.0 A, resolution. Remarkably, the polypeptide connecting the two halves of the, Rossmann fold exposes two identical knuckles related by a 2-fold axis but, with zinc in the distal knuckle only. Examination of available MetRS, orthologs reveals four classes according to the number and zinc content of, the putative knuckles. Extreme cases are exemplified by the MetRS of, eucaryotic or archaeal origin, where two knuckles and two metal ions are, expected, and by the mitochondrial enzymes, which are predicted to have, one knuckle without metal ion.

About this Structure

1QQT is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as Methionine--tRNA ligase, with EC number 6.1.1.10 Full crystallographic information is available from OCA.

Reference

Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features., Mechulam Y, Schmitt E, Maveyraud L, Zelwer C, Nureki O, Yokoyama S, Konno M, Blanquet S, J Mol Biol. 1999 Dec 17;294(5):1287-97. PMID:10600385

Page seeded by OCA on Wed Nov 21 00:54:12 2007

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