1yn9

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[[Image:1yn9.gif|left|200px]]
[[Image:1yn9.gif|left|200px]]
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{{Structure
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|PDB= 1yn9 |SIZE=350|CAPTION= <scene name='initialview01'>1yn9</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1yn9", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_5'-phosphatase Polynucleotide 5'-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.33 3.1.3.33] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PTP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46015 Autographa californica nucleopolyhedrovirus])
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|DOMAIN=
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{{STRUCTURE_1yn9| PDB=1yn9 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yn9 OCA], [http://www.ebi.ac.uk/pdbsum/1yn9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yn9 RCSB]</span>
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'''Crystal structure of baculovirus RNA 5'-phosphatase complexed with phosphate'''
'''Crystal structure of baculovirus RNA 5'-phosphatase complexed with phosphate'''
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[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: Shuman, S.]]
[[Category: Shuman, S.]]
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[[Category: cysteine phosphatase]]
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[[Category: Cysteine phosphatase]]
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[[Category: p-loop]]
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[[Category: P-loop]]
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[[Category: rna triphosphatase]]
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[[Category: Rna triphosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:32:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:14:06 2008''
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Revision as of 13:32, 3 May 2008

Template:STRUCTURE 1yn9

Crystal structure of baculovirus RNA 5'-phosphatase complexed with phosphate


Overview

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 A resolution. BVP adopts the characteristic cysteine-phosphatase alpha/beta 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 (118)HCTHGXNRT(126) 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.

About this Structure

1YN9 is a Single protein structure of sequence from Autographa californica nucleopolyhedrovirus. Full crystallographic information is available from OCA.

Reference

Crystal structure of baculovirus RNA triphosphatase complexed with phosphate., Changela A, Martins A, Shuman S, Mondragon A, J Biol Chem. 2005 May 6;280(18):17848-56. Epub 2005 Feb 15. PMID:15713658 Page seeded by OCA on Sat May 3 16:32:11 2008

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