Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation.

Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Research Abstract Details 

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Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Abstract Text:

Melissa M Getz,Andy J Andrews,Carol A Fierke,Hashim M Al-Hashimi,

The P4 helix is an essential element of ribonuclease P (RNase P) that is believed to bind catalytically important metals. Here, we applied a combination of NMR residual dipolar couplings (RDCs) and a recently introduced domain-elongation strategy for measuring "motionally decoupled" relaxation data to characterize the structural dynamics of the P4 helix from Bacillus subtilis RNase P. In the absence of divalent ions, the two P4 helical domains undergo small amplitude (approximately 13 degrees) collective motions about an average interhelical angle of 10 degrees. The highly conserved U7 bulge and helical residue C8, which are proposed to be important for substrate recognition and metal binding, are locally mobile at pico- to nanosecond timescales and together form the pivot point for the collective domain motions. Chemical shift mapping reveals significant association of Mg2+ ions at the P4 major groove near the flexible pivot point at residues (A5, G22, G23) previously identified to bind catalytically important metals. The Mg2+ ions do not, however, significantly alter the structure or dynamics of P4. Analysis of results in the context of available X-ray structures of the RNA component of RNase P and structural models that include the pre-tRNA substrate suggest that the internal motions observed in P4 likely facilitate adaptive changes in conformation that take place during folding and substrate recognition, possibly aided by interactions with Mg2+ ions. Our results add to a growing view supporting the existence of functionally important internal motions in RNA occurring at nanosecond timescales.

Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Publishing Authors By Initials

MM Getz,AJ Andrews,CA Fierke,HM Al-Hashimi,

For similar ribonuclease p research abstracts see: ribonuclease p research

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Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: RNA (New York, N.Y.)

VOLUME: 13

Page Numbers: 251-66

Journal Abbreviation: RNA

ISSN: 1355-8382

DAY: 28

MONTH: 12

YEAR: 2006

Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Information

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LANGUAGE: eng

NlmUniqueID: 9509184

Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Keywords Mesh Terms:

KEYWORDS: Ribonuclease P

MESH TERMS: metabolism

Chemical & Substance for Abstract: Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation. Information

Substance Name: Ribonuclease P

Registry Number: EC 3.1.26.5

Grant and Affiliation Information for Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxation.

AFFILIATION: Department of Chemistry, University of Michigan, Ann Arbor 48109, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: R01 GM55387

ACRONYM: GM

MEDLINETA: RNA

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