2a64: Difference between revisions

Revision as of 17:24, 21 February 2008

Crystal Structure of Bacterial Ribonuclease P RNA

OverviewOverview

The x-ray crystal structure of a 417-nt ribonuclease P RNA from Bacillus stearothermophilus was solved to 3.3-A resolution. This RNA enzyme is constructed from a number of coaxially stacked helical domains joined together by local and long-range interactions. These helical domains are arranged to form a remarkably flat surface, which is implicated by a wealth of biochemical data in the binding and cleavage of the precursors of transfer RNA substrate. Previous photoaffinity crosslinking data are used to position the substrate on the crystal structure and to identify the chemically active site of the ribozyme. This site is located in a highly conserved core structure formed by intricately interlaced long-range interactions between interhelical sequences.

About this StructureAbout this Structure

2A64 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of a bacterial ribonuclease P RNA., Kazantsev AV, Krivenko AA, Harrington DJ, Holbrook SR, Adams PD, Pace NR, Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13392-7. Epub 2005 Sep 12. PMID:16157868

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OCA

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 ==Overview==
-The x-ray crystal structure of a 417-nt ribonuclease P RNA from Bacillus, stearothermophilus was solved to 3.3-A resolution. This RNA enzyme is, constructed from a number of coaxially stacked helical domains joined, together by local and long-range interactions. These helical domains are, arranged to form a remarkably flat surface, which is implicated by a, wealth of biochemical data in the binding and cleavage of the precursors, of transfer RNA substrate. Previous photoaffinity crosslinking data are, used to position the substrate on the crystal structure and to identify, the chemically active site of the ribozyme. This site is located in a, highly conserved core structure formed by intricately interlaced, long-range interactions between interhelical sequences.
+The x-ray crystal structure of a 417-nt ribonuclease P RNA from Bacillus stearothermophilus was solved to 3.3-A resolution. This RNA enzyme is constructed from a number of coaxially stacked helical domains joined together by local and long-range interactions. These helical domains are arranged to form a remarkably flat surface, which is implicated by a wealth of biochemical data in the binding and cleavage of the precursors of transfer RNA substrate. Previous photoaffinity crosslinking data are used to position the substrate on the crystal structure and to identify the chemically active site of the ribozyme. This site is located in a highly conserved core structure formed by intricately interlaced long-range interactions between interhelical sequences.
 ==About this Structure==
@@ Line 12: / Line 12: @@
 Crystal structure of a bacterial ribonuclease P RNA., Kazantsev AV, Krivenko AA, Harrington DJ, Holbrook SR, Adams PD, Pace NR, Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13392-7. Epub 2005 Sep 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16157868 16157868]
 [[Category: Single protein]]
-[[Category: Adams, P.D.]]
+[[Category: Adams, P D.]]
-[[Category: Harrington, D.J.]]
+[[Category: Harrington, D J.]]
-[[Category: Holbrook, S.R.]]
+[[Category: Holbrook, S R.]]
-[[Category: Kazantsev, A.V.]]
+[[Category: Kazantsev, A V.]]
-[[Category: Krivenko, A.A.]]
+[[Category: Krivenko, A A.]]
-[[Category: Pace, N.R.]]
+[[Category: Pace, N R.]]
 [[Category: hydrolase]]
 [[Category: ribonuclease]]
 [[Category: ribozyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:55:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:00 2008''