1r6l: Difference between revisions

Revision as of 15:47, 29 July 2008

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File:1r6l.png

Template:STRUCTURE 1r6l

Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas AeruginosaCrystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa

Template:ABSTRACT PUBMED 14573594

About this StructureAbout this Structure

1R6L is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

Probing the functional importance of the hexameric ring structure of RNase PH., Choi JM, Park EY, Kim JH, Chang SK, Cho Y, J Biol Chem. 2004 Jan 2;279(1):755-64. Epub 2003 Oct 22. PMID:14573594

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OCA

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-[[Image:1r6l.gif|left|200px]]
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-'''Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa'''
+===Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa===
-==Overview==
+<!--
-RNase PH is a phosphate-dependent exoribonuclease that catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process. The 1.9-A crystal structures of the apo and the phosphate-bound forms of RNase PH from Pseudomonas aeruginosa reveal a monomeric RNase PH with an alpha/beta-fold tightly associated into a hexameric ring structure in the form of a trimer of dimers. A five ion pair network, Glu-63-Arg-74-Asp-116-Arg-77-Asp-118 and an ion-pair Glu-26-Arg-69 that are positioned symmetrically in the trimerization interface play critical roles in the formation of a hexameric ring. Single or double mutations of Arg-69, Arg-74, or Arg-77 in these ion pairs leads to the dissociation of the RNase PH hexamer into dimers without perturbing the overall monomeric structure. The dissociated RNase PH dimer completely lost its binding affinity and catalytic activity against a precursor tRNA. Our structural and mutational analyses of RNase PH demonstrate that the hexameric ring formation is a critical feature for the function of members of the RNase PH family.
+The line below this paragraph, {{ABSTRACT_PUBMED_14573594}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14573594 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14573594}}
 ==About this Structure==
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 [[Category: Hexamer]]
 [[Category: Phosphate bound]]
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