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Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution.

Pletinckx J, Steyaert J, Zegers I, Choe HW, Heinemann U, Wyns L
Biochemistry 33 1654-62 (1994)
Cited: 7 times
EuropePMC logo PMID: 7906540

Abstract

Glu58 is known to participate in phosphodiester transesterification catalyzed by the enzyme RNase T1. For Glu58 RNase T1, an altered mechanism has been proposed in which His40 replaces Glu58 as the base catalyst [Steyaert, J., Hallenga, K., Wyns, L., & Stanssens, P. (1990) Biochemistry 29, 9064-9072]. Glu58Ala Rnase T1 has been cocrystallized with guanosine 2'-monophosphate (2'-GMP). The crystals are of space group P2(1), with one molecule per asymmetric unit (a = 32.44 A, b = 49.64 A, c = 26.09 A, beta = 99.17 degrees). The three-dimensional structure of the enzyme was determined to a nominal resolution of 1.9 A, yielding a crystallographic R factor of 0.178 for all X-ray data. Comparison of this structure with wild-type structures leads to the following conclusions. The minor changes apparent in the tertiary structure can be explained by either the mutation of Glu58 or by the change in the space group. In the active site, the extra space available through the mutation of Glu58 is occupied by the phosphate group (after a reorientation) and by a solvent molecule replacing a carboxylate oxygen of Glu58. This solvent molecule is a candidate for participation in the altered mechanism of this mutant enzyme. Following up on a study of conserved water sites in RNase T1 crystallized in space group P2(1)2(1)2(1) [Malin, R., Zielenkiewicz, P., & Saenger, W. (1991) J. Mol. Biol. 266, 4848-4852], we investigated the hydration structure for four different packing modes of RNase T1.(ABSTRACT TRUNCATED AT 250 WORDS)

Articles - 1lra mentioned but not cited (1)

  1. Multiple structural alignment by secondary structures: algorithm and applications. Dror O, Benyamini H, Nussinov R, Wolfson HJ. Protein Sci 12 2492-2507 (2003)


Reviews citing this publication (2)

  1. A decade of protein engineering on ribonuclease T1--atomic dissection of the enzyme-substrate interactions. Steyaert J. Eur. J. Biochem. 247 1-11 (1997)
  2. Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidases. Takahashi K. Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 89 201-225 (2013)

Articles citing this publication (4)

  1. The structures of RNase A complexed with 3'-CMP and d(CpA): active site conformation and conserved water molecules. Zegers I, Maes D, Dao-Thi MH, Poortmans F, Palmer R, Wyns L. Protein Sci. 3 2322-2339 (1994)
  2. Are turns required for the folding of ribonuclease T1? Garrett JB, Mullins LS, Raushel FM. Protein Sci. 5 204-211 (1996)
  3. Conserved water molecules in a large family of microbial ribonucleases. Loris R, Langhorst U, De Vos S, Decanniere K, Bouckaert J, Maes D, Transue TR, Steyaert J. Proteins 36 117-134 (1999)
  4. Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond. Loverix S, Winqvist A, Strömberg R, Steyaert J. Chem. Biol. 7 651-658 (2000)


Related citations provided by authors (9)

  1. Three-Dimensional Structure of Ribonuclease T1 Complexed with Guanylyl-2',5'-Guanosine at 1.8 Angstroms Resolution. Koepke J, Maslowska M, Heinemann U, Saenger W J. Mol. Biol. 206 475- (1989)
  2. Three-Dimensional Structure of the Ribonuclease T1(Asterisk)2'-Gmp Complex at 1.9-Angstroms Resolution. Arni R, Heinemann U, Tokuoka R, Saenger W J. Biol. Chem. 263 15358- (1988)
  3. Restrained Least-Squares Refinement of the Crystal Structure of the Ribonuclease T1(Asterisk)2'-Guanylic Acid Complex at 1.9 Angstroms Resolution. Arni R, Heinemann U, Maslowska M, Tokuoka R, Saenger W Acta Crystallogr., B 43 549- (1987)
  4. The Structural and Sequence Homology of a Family of Microbial Ribonucleases. Hill C, Dodson G, Heinemann U, Saenger W, Mitsui Y, Nakamura K, Borisov S, Tischenko G, Polyakov K, Pavlovsky S Trends Biochem. Sci. (Pers. Ed. ) 8 364- (1983)
  5. Crystallographic study of mechanism of ribonuclease T1-catalysed specific RNA hydrolysis.. Heinemann U, Saenger W J Biomol Struct Dyn 1 523-38 (1983)
  6. Specific Protein-Nucleic Acid Recognition in Ribonuclease T1-2'-Guanylic Acid Complex. An X-Ray Study. Heinemann U, Saenger W Nature 299 27- (1982)
  7. Crystallization of a Complex between Ribonuclease T1 and 2'-Guanylic Acid. Heinemann U, Wernitz M, Paehler A, Saenger W, Menke G, Rueterjans H Eur. J. Biochem. 109 109- (1980)
  8. Ribonuclease T1 with Free Recognition and Catalytic Site: Crystal Structure Analysis at 1.5 Angstroms. Martinez-Oyanedel J, Choe H-W, Heinemann U, Saenger W J. Mol. Biol. 222 335- (1991)
  9. Histidine-40 of Ribonuclease T1Acts as Base Catalyst When the True Catalytic Base, Glutamic Acid 58 is Replaced by Alanine. Steyaert J, Hallenga K, Wyns L, Stanssens P Biochemistry 29 9064- (1990)

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