1r6m: Difference between revisions
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[[Image:1r6m.jpg|left|200px]]<br /><applet load="1r6m" size=" | [[Image:1r6m.jpg|left|200px]]<br /><applet load="1r6m" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1r6m, resolution 2.00Å" /> | caption="1r6m, resolution 2.00Å" /> | ||
'''Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa In Complex With Phosphate'''<br /> | '''Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa In Complex With Phosphate'''<br /> | ||
==Overview== | ==Overview== | ||
RNase PH is a phosphate-dependent exoribonuclease that catalyzes the | 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. | ||
==About this Structure== | ==About this Structure== | ||
1R6M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/tRNA_nucleotidyltransferase tRNA nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.56 2.7.7.56] Full crystallographic information is available from [http:// | 1R6M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/tRNA_nucleotidyltransferase tRNA nucleotidyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.56 2.7.7.56] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6M OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: tRNA nucleotidyltransferase]] | [[Category: tRNA nucleotidyltransferase]] | ||
[[Category: Chang, S | [[Category: Chang, S K.]] | ||
[[Category: Cho, Y.]] | [[Category: Cho, Y.]] | ||
[[Category: Choi, J | [[Category: Choi, J M.]] | ||
[[Category: Kim, J | [[Category: Kim, J H.]] | ||
[[Category: Park, E | [[Category: Park, E Y.]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: beta-alpha-beta-alpha fold]] | [[Category: beta-alpha-beta-alpha fold]] | ||
| Line 24: | Line 24: | ||
[[Category: phosphate bound]] | [[Category: phosphate bound]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:37 2008'' | ||
Revision as of 15:47, 21 February 2008
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Crystal Structure Of The tRNA Processing Enzyme Rnase pH From Pseudomonas Aeruginosa In Complex With Phosphate
OverviewOverview
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.
About this StructureAbout this Structure
1R6M is a Single protein structure of sequence from Pseudomonas aeruginosa with as ligand. Active as tRNA nucleotidyltransferase, with EC number 2.7.7.56 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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