1rbj: Difference between revisions
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rb/1rbj_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rb/1rbj_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rbj ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rbj ConSurf]. | ||
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== Publication Abstract from PubMed == | |||
The structure of a tetragonal crystal of bovine pancreatic RNase B complexed with d(pA)(4) was determined by molecular replacement and difference Fourier methods. This crystal belongs to space group P4(1)2(1)2 and has unit-cell dimensions a = b = 44.5, c = 156.5 A. The model consists of the enzyme and a tetranucleotide with fractional occupancies, suggesting multiple modes of oligonucleotide binding. It does not include any polysaccharide residues or solvent molecules. After refinement at 2.7 A, the R value was 0.163 with acceptable stereochemistry. The model illustrates a set of well defined interactions for substrate binding, particularly between the central dinucleotide and the enzyme. | |||
Structure of a ribonuclease B+d(pA)4 complex.,Ko TP, Williams R, McPherson A Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):160-4. PMID:15299737<ref>PMID:15299737</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 1rbj" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Latest revision as of 07:51, 17 October 2024
RIBONUCLEASE B COMPLEX WITH D(TETRA-(DEOXY-ADENYLATE))RIBONUCLEASE B COMPLEX WITH D(TETRA-(DEOXY-ADENYLATE))
Structural highlights
FunctionRNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of a tetragonal crystal of bovine pancreatic RNase B complexed with d(pA)(4) was determined by molecular replacement and difference Fourier methods. This crystal belongs to space group P4(1)2(1)2 and has unit-cell dimensions a = b = 44.5, c = 156.5 A. The model consists of the enzyme and a tetranucleotide with fractional occupancies, suggesting multiple modes of oligonucleotide binding. It does not include any polysaccharide residues or solvent molecules. After refinement at 2.7 A, the R value was 0.163 with acceptable stereochemistry. The model illustrates a set of well defined interactions for substrate binding, particularly between the central dinucleotide and the enzyme. Structure of a ribonuclease B+d(pA)4 complex.,Ko TP, Williams R, McPherson A Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):160-4. PMID:15299737[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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