1buj

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(New page: 200px<br /><applet load="1buj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buj" /> '''STRUCTURE OF BINASE IN SOLUTION'''<br /> ==...)
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[[Image:1buj.jpg|left|200px]]<br /><applet load="1buj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1buj" />
 
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'''STRUCTURE OF BINASE IN SOLUTION'''<br />
 
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==Overview==
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==STRUCTURE OF BINASE IN SOLUTION==
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We present the spatial structure of binase, a small extracellular, ribonuclease, derived from 1H-NMR* data in aqueous solution. The total of, 20 structures were obtained via torsion angle dynamics using DYANA program, with experimental NOE and hydrogen bond distance constraints and phi and, chi1 dihedral angle constraints. The final structures were energy, minimised with ECEPP/2 potential in FANTOM program. Binase consists of, three alpha-helices in N-terminal part (residues 6-16, 26-32 and 41-44), five-stranded antiparallel beta-sheet in C-terminal part (residues 51-55, 70-75, 86-90, 94-99 and 104-108) and two-stranded parallel beta-sheet, (residues 22-24 and 49-51). Three loops (residues 36-39, 56-67 and 76-83), which play significant role in biological functioning of binase, are, flexible in solution. The differences between binase and barnase spatial, structures in solution explain the differences in thermostability of, binase, barnase and their hybrids.
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<StructureSection load='1buj' size='340' side='right'caption='[[1buj]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1buj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1buj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buj OCA], [https://pdbe.org/1buj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1buj RCSB], [https://www.ebi.ac.uk/pdbsum/1buj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1buj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RN_BACIN RN_BACIN] This is a purine-specific ribonuclease.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1buj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1buj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We present the spatial structure of binase, a small extracellular ribonuclease, derived from 1H-NMR* data in aqueous solution. The total of 20 structures were obtained via torsion angle dynamics using DYANA program with experimental NOE and hydrogen bond distance constraints and phi and chi1 dihedral angle constraints. The final structures were energy minimised with ECEPP/2 potential in FANTOM program. Binase consists of three alpha-helices in N-terminal part (residues 6-16, 26-32 and 41-44), five-stranded antiparallel beta-sheet in C-terminal part (residues 51-55, 70-75, 86-90, 94-99 and 104-108) and two-stranded parallel beta-sheet (residues 22-24 and 49-51). Three loops (residues 36-39, 56-67 and 76-83), which play significant role in biological functioning of binase, are flexible in solution. The differences between binase and barnase spatial structures in solution explain the differences in thermostability of binase, barnase and their hybrids.
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==About this Structure==
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Three-dimensional structure of binase in solution.,Reibarkh MYa, Nolde DE, Vasilieva LI, Bocharov EV, Shulga AA, Kirpichnikov MP, Arseniev AS FEBS Lett. 1998 Jul 17;431(2):250-4. PMID:9708913<ref>PMID:9708913</ref>
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1BUJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BUJ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Three-dimensional structure of binase in solution., Reibarkh MYa, Nolde DE, Vasilieva LI, Bocharov EV, Shulga AA, Kirpichnikov MP, Arseniev AS, FEBS Lett. 1998 Jul 17;431(2):250-4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9708913 9708913]
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</div>
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[[Category: Bacillus intermedius]]
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<div class="pdbe-citations 1buj" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Arseniev, A.S.]]
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[[Category: Nolde, D.E.]]
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[[Category: Reibarkh, M.Y.]]
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[[Category: Vasilieva, L.I.]]
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[[Category: microbial ribonuclease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:56:04 2007''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus intermedius]]
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[[Category: Large Structures]]
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[[Category: Arseniev AS]]
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[[Category: Nolde DE]]
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[[Category: Reibarkh MY]]
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[[Category: Vasilieva LI]]

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STRUCTURE OF BINASE IN SOLUTION

PDB ID 1buj

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