Crystal structure of baculovirus RNA triphosphatase complexed with phosphate Journal Article
| Authors: | Changela, A.; Martins, A.; Shuman, S.; Mondragón, A. |
| Article Title: | Crystal structure of baculovirus RNA triphosphatase complexed with phosphate |
| Abstract: | Baculovirus RNA 5′-triphosphatase (BVP) exemplifies a family of RNA-specific cysteine phosphatases that includes the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. Here we report the crystal structure of BVP in a phosphate-bound state at 1.5 Å resolution. BVP adopts the characteristic cysteine-phosphatase α/β fold and binds two phosphate ions in the active site region, one of which is proposed to mimic the phosphate of the product complex after hydrolysis of the covalent phosphoenzyme intermediate. The crystal structure highlights the role of backbone amides and side chains of the P-loop motif 118HCTHGXNRT126 in binding the cleavable phosphate and stabilizing the transition state. Comparison of the BVP structure to the apoenzyme of mammalian RNA triphosphatase reveals a concerted movement of the Arg-125 side chain (to engage the phosphate directly) and closure of an associated surface loop over the phosphate in the active site. The structure highlights a direct catalytic role of Asn-124, which is the signature P-loop residue of the RNA triphosphatase family and a likely determinant of the specificity of BVP for hydrolysis of phosphoanhydride linkages. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc. |
| Keywords: | unclassified drug; genetics; nonhuman; molecular genetics; protein domain; mouse; metabolism; mammalia; phosphatase; protein binding; enzymology; acid anhydride hydrolase; rna triphosphatase; acid anhydride hydrolases; physiology; rna; chemistry; amino acid sequence; molecular sequence data; messenger rna; virus rna; binding site; crystal structure; crystallography, x-ray; binding energy; binding sites; catalysis; molecular biology; protein family; crystallization; x ray crystallography; enzyme structure; biochemistry; alpha chain; phosphate; phosphates; hydrolysis; enzymes; arginine; asparagine; rna, viral; side chains; enzyme active site; amide; metazoa; enzyme stability; beta chain; baculovirus; virus enzyme; baculoviridae; acid anhydride; metazoon; phosphate-bound state; phosphoanhydride; apoenzyme; baculovirus rna triphosphatase; cysteine phosphatase |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 280 |
| Issue: | 18 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2005-05-06 |
| Start Page: | 17848 |
| End Page: | 17856 |
| Language: | English |
| DOI: | 10.1074/jbc.M500885200 |
| PUBMED: | 15713658 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | --- - "Cited By (since 1996): 10" - "Export Date: 24 October 2012" - "CODEN: JBCHA" - "Source: Scopus" |
Altmetric
Citation Impact
BMJ Impact Analytics
Related MSK Work