2rbi

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[[Image:2rbi.jpg|left|200px]]
[[Image:2rbi.jpg|left|200px]]
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{{Structure
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|PDB= 2rbi |SIZE=350|CAPTION= <scene name='initialview01'>2rbi</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_2rbi", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=1:Catalytic+Site+Residues'>1</scene>, <scene name='pdbsite=2:Mutated+Catalytic+Site+Residue'>2</scene> and <scene name='pdbsite=3:Main+Nucleotide+Binding+Residue'>3</scene>
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|GENE= PHOA-BINASE HIS101ASN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1400 Bacillus intermedius])
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|DOMAIN=
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{{STRUCTURE_2rbi| PDB=2rbi | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rbi OCA], [http://www.ebi.ac.uk/pdbsum/2rbi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rbi RCSB]</span>
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'''STRUCTURE OF BINASE MUTANT HIS 101 ASN'''
'''STRUCTURE OF BINASE MUTANT HIS 101 ASN'''
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[[Category: Offen, W A.]]
[[Category: Offen, W A.]]
[[Category: Okorokov, A L.]]
[[Category: Okorokov, A L.]]
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[[Category: endoribonuclease]]
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[[Category: Endoribonuclease]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: microbial extracellular ribonuclease]]
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[[Category: Microbial extracellular ribonuclease]]
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[[Category: phosphodiester transferase]]
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[[Category: Phosphodiester transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:36:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:58:34 2008''
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Revision as of 13:36, 4 May 2008

Image:2rbi.jpg

Template:STRUCTURE 2rbi

STRUCTURE OF BINASE MUTANT HIS 101 ASN


Overview

Members of the microbial guanyl-specific ribonuclease family catalyse the endonucleolytic cleavage of single-stranded RNA in a two-step reaction involving transesterification to form a 2',3'-cyclic phosphate and its subsequent hydrolysis to yield the respective 3'-phosphate. The extracellular ribonuclease from Bacillus intermedius (binase, RNase Bi) shares a common mechanism for RNA hydrolysis with mammalian RNases. Two catalytic residues in the active site of binase, Glu72 and His101, are thought to be involved in general acid-general base catalysis of RNA cleavage. Using site-directed mutagenesis, binase mutants were produced containing amino acid substitutions H101N and H101T and their catalytic properties towards RNA, poly(I), poly(A), GpC and guanosine 2',3'-cyclic phosphate (cGMP) substrates were studied. The engineered mutant proteins are active in the transesterification step which produces the 2',3'-cyclic phosphate species but they have lost the ability to catalyse hydrolysis of the cyclic phosphate to give the 3' monophosphate product.

About this Structure

2RBI is a Single protein structure of sequence from Bacillus intermedius. Full crystallographic information is available from OCA.

Reference

RNA cleavage without hydrolysis. Splitting the catalytic activities of binase with Asn101 and Thr101 mutations., Okorokov AL, Panov KI, Offen WA, Mukhortov VG, Antson AA, Karpeisky MYa, Wilkinson AJ, Dodson GG, Protein Eng. 1997 Mar;10(3):273-8. PMID:9153077 Page seeded by OCA on Sun May 4 16:36:31 2008

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