4hwp: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4hwp|  PDB=4hwp  |  SCENE=  }}
===Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor===
{{ABSTRACT_PUBMED_23362938}}


The entry 4hwp is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/SYT_ECOLI SYT_ECOLI]] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]


Authors: Hilgers, M.T.
==About this Structure==
[[4hwp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWP OCA].  


Description: Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor
==Reference==
<ref group="xtra">PMID:023362938</ref><references group="xtra"/><references/>
[[Category: Escherichia coli k-12]]
[[Category: Threonine--tRNA ligase]]
[[Category: Hilgers, M T.]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Antibacterial]]
[[Category: Ligase-ligase inhibitor complex]]
[[Category: Protein-inhibitor complex]]

Revision as of 04:13, 20 September 2013

Template:STRUCTURE 4hwp

Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor

Template:ABSTRACT PUBMED 23362938

Function

[SYT_ECOLI] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]

About this Structure

4hwp is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

Reference

  1. Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J. Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design. J Med Chem. 2013 Feb 28;56(4):1748-60. doi: 10.1021/jm301756m. Epub 2013 Feb 12. PMID:23362938 doi:10.1021/jm301756m

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