4a91

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m (Protected "4a91" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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[[Image:4a91.png|left|200px]]
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The entry 4a91 is ON HOLD
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{{STRUCTURE_4a91| PDB=4a91 | SCENE= }}
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Authors: Blaise, M., Olieric, V., Sauter, C., Lorber, B., Roy, B., Karmakar, S., Banerjee, R., Becker, H.D., Kern, D., ,
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===Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate===
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Description: Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate
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{{ABSTRACT_PUBMED_18602926}}
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==About this Structure==
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[[4a91]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zlz 2zlz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A91 OCA].
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==Reference==
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<ref group="xtra">PMID:018602926</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Banerjee, R.]]
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[[Category: Becker, H D.]]
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[[Category: Blaise, M.]]
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[[Category: Karmakar, S.]]
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[[Category: Kern, D.]]
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[[Category: Lorber, B.]]
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[[Category: Olieric, V.]]
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[[Category: Roy, B.]]
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[[Category: Sauter, C.]]
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[[Category: Ligase]]

Revision as of 06:15, 11 January 2012

Template:STRUCTURE 4a91

Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate

Template:ABSTRACT PUBMED 18602926

About this Structure

4a91 is a 1 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2zlz. Full crystallographic information is available from OCA.

Reference

  • Blaise M, Olieric V, Sauter C, Lorber B, Roy B, Karmakar S, Banerjee R, Becker HD, Kern D. Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. J Mol Biol. 2008 Sep 19;381(5):1224-37. Epub 2008 Jun 26. PMID:18602926 doi:10.1016/j.jmb.2008.06.053

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