4jg4

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'''Unreleased structure'''
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{{STRUCTURE_4jg4| PDB=4jg4 | SCENE= }}
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===Ligand concentration regulates the pathways of coupled protein folding and binding===
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{{ABSTRACT_PUBMED_24364358}}
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The entry 4jg4 is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/G4ENZ9_BACIU G4ENZ9_BACIU]] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme (By similarity).[HAMAP-Rule:MF_00227][SAAS:SAAS000100_004_060152]
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Authors: Tonthat, N.K.
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==About this Structure==
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[[4jg4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JG4 OCA].
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Description: Ligand concentration regulates the pathways of coupled protein folding and binding
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==Reference==
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<ref group="xtra">PMID:024364358</ref><references group="xtra"/><references/>
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[[Category: Ribonuclease P]]
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[[Category: Tonthat, N K.]]
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[[Category: Endonuclease]]
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[[Category: Hydrolase]]
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[[Category: Rna-binding]]

Revision as of 06:55, 22 January 2014

Template:STRUCTURE 4jg4

Contents

Ligand concentration regulates the pathways of coupled protein folding and binding

Template:ABSTRACT PUBMED 24364358

Function

[G4ENZ9_BACIU] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme (By similarity).[HAMAP-Rule:MF_00227][SAAS:SAAS000100_004_060152]

About this Structure

4jg4 is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Daniels KG, Tonthat NK, McClure DR, Chang YC, Liu X, Schumacher MA, Fierke CA, Schmidler SC, Oas TG. Ligand Concentration Regulates the Pathways of Coupled Protein Folding and Binding. J Am Chem Soc. 2014 Jan 9. PMID:24364358 doi:http://dx.doi.org/10.1021/ja4086726

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