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3pd2

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'''Unreleased structure'''
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{{Seed}}
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[[Image:3pd2.jpg|left|200px]]
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The entry 3pd2 is ON HOLD until Paper Publication
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{{STRUCTURE_3pd2| PDB=3pd2 | SCENE= }}
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Authors: Hussain, T., Kamarthapu, V., Kruparani, S.P., Sankaranarayanan, R.
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===Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine===
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Description: Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 13:57:31 2010''
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(as it appears on PubMed at http://www.pubmed.gov), where 21098258 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21098258}}
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==About this Structure==
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3PD2 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PD2 OCA].
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==Reference==
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<ref group="xtra">PMID:21098258</ref><references group="xtra"/>
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[[Category: Pyrococcus abyssi]]
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[[Category: Threonine--tRNA ligase]]
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[[Category: Hussain, T.]]
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[[Category: Kamarthapu, V.]]
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[[Category: Kruparani, S P.]]
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[[Category: Sankaranarayanan, R.]]
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[[Category: Alpha/beta fold]]
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[[Category: Aminoacyl-trna synthetase]]
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[[Category: Deacylase]]
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[[Category: Editing]]
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[[Category: Ligase]]
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[[Category: Translation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:54:23 2010''

Revision as of 08:42, 8 December 2010

Template:STRUCTURE 3pd2

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine

Template:ABSTRACT PUBMED 21098258

About this Structure

3PD2 is a 2 chains structure with sequences from Pyrococcus abyssi. Full crystallographic information is available from OCA.

Reference

  • Hussain T, Kamarthapu V, Kruparani SP, Deshmukh MV, Sankaranarayanan R. Mechanistic insights into cognate substrate discrimination during proofreading in translation. Proc Natl Acad Sci U S A. 2010 Nov 22. PMID:21098258 doi:10.1073/pnas.1014299107

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