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1nzj

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[[Image:1nzj.gif|left|200px]]<br /><applet load="1nzj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nzj.gif|left|200px]]
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caption="1nzj, resolution 1.50&Aring;" />
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'''Crystal Structure and Activity Studies of Escherichia Coli Yadb ORF'''<br />
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{{Structure
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|PDB= 1nzj |SIZE=350|CAPTION= <scene name='initialview01'>1nzj</scene>, resolution 1.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal Structure and Activity Studies of Escherichia Coli Yadb ORF'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1NZJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZJ OCA].
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1NZJ 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=1NZJ OCA].
==Reference==
==Reference==
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The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity., Campanacci V, Dubois DY, Becker HD, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giege R, Cambillau C, J Mol Biol. 2004 Mar 19;337(2):273-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15003446 15003446]
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The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity., Campanacci V, Dubois DY, Becker HD, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giege R, Cambillau C, J Mol Biol. 2004 Mar 19;337(2):273-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15003446 15003446]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ZN]]
[[Category: ZN]]
[[Category: glutamyl t-rna synthetase]]
[[Category: glutamyl t-rna synthetase]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: zn cluster]]
[[Category: zn cluster]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:11:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:03:45 2008''

Revision as of 11:03, 20 March 2008


PDB ID 1nzj

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



Crystal Structure and Activity Studies of Escherichia Coli Yadb ORF


Overview

In the course of a structural genomics program aiming at solving the structures of Escherichia coli open reading frame products of unknown function, we have determined the structure of YadB at 1.5A using molecular replacement. The YadB protein is 298 amino acid residues long and displays 34% sequence identity with E.coli glutamyl-tRNA synthetase (GluRS). It is much shorter than GluRS, which contains 468 residues, and lacks the complete domain interacting with the tRNA anticodon loop. As E.coli GluRS, YadB possesses a Zn2+ located in the putative tRNA acceptor stem-binding domain. The YadB cluster uses cysteine residues as the first three zinc ligands, but has a weaker tyrosine ligand at the fourth position. It shares with canonical amino acid RNA synthetases a major functional feature, namely activation of the amino acid (here glutamate). It differs, however, from GluRSs by the fact that the activation step is tRNA-independent and that it does not catalyze attachment of the activated glutamate to E.coli tRNAGlu, but to another, as yet unknown tRNA. These results suggest thus a novel function, distinct from that of GluRSs, for the yadB gene family.

About this Structure

1NZJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity., Campanacci V, Dubois DY, Becker HD, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giege R, Cambillau C, J Mol Biol. 2004 Mar 19;337(2):273-83. PMID:15003446

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