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1bao

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[[Image:1bao.gif|left|200px]]
 
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==THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS==
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The line below this paragraph, containing "STRUCTURE_1bao", creates the "Structure Box" on the page.
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<StructureSection load='1bao' size='340' side='right'caption='[[1bao]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1bao]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BAO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1bao| PDB=1bao | SCENE= }}
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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=1bao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bao OCA], [https://pdbe.org/1bao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bao RCSB], [https://www.ebi.ac.uk/pdbsum/1bao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bao ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.
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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/ba/1bao_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=1bao ConSurf].
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<div style="clear:both"></div>
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'''THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS'''
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==See Also==
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*[[Barnase 3D structures|Barnase 3D structures]]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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==Overview==
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__TOC__
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The crystal structures of two barnase mutants, Tyr78--&gt;Phe and Ser91--&gt;Ala, have been determined to 2.2 A resolution. In both cases, a buried hydroxyl group that makes two hydrogen bonds within the protein was replaced by a hydrogen atom. It is found that neither mutation causes any structural changes, within the limits of error, compared with wild-type and so are confirmed to be non-disruptive. Solvent molecules are not observed in the cavities created by removal of the respective hydroxyl groups and no new interactions are introduced. The local water structure surrounding both sites of mutation is well conserved and resembles that of the wild-type. All four water molecules making contacts with the side-chain of residue 78 and two water molecules nearest to residue 91 in the wild-type are found within a sphere of 0.5 A radius, at the equivalent positions of the respective mutant. No new water molecules are found bound to any of the hydrogen bond donor or acceptor residues involved in these two mutation sites. Previous protein engineering experiments established that the solvent-inaccessible phenolic OH of Tyr78 that makes hydrogen bonds with two uncharged groups (main-chain NH and CO) contributes 1.4 kcal mol-1 to protein stability, while the solvent-inaccessible OH of Ser91 that makes hydrogen bonds with an uncharged main-chain NH and a charged group (O gamma 1) contributes 1.9 kcal mol-1. These stability measurements can now be attributed primarily to the loss of the hydrogen bonding interactions because both mutations neither disrupt the respective protein and local solvent structures, upset the overall hydrogen bonding pattern nor introduce new interactions. The mutations Tyr78--&gt;Phe and Ser91--&gt;Ala are thus good examples of "non-disruptive deletions" and the results of mutagenesis can be analysed at the simplest level.
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</StructureSection>
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==About this Structure==
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1BAO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAO OCA].
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==Reference==
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Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants., Chen YW, Fersht AR, Henrick K, J Mol Biol. 1993 Dec 20;234(4):1158-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8263918 8263918]
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[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Chen, Y W.]]
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[[Category: Chen YW]]
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[[Category: Fersht, A R.]]
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[[Category: Fersht AR]]
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[[Category: Henrick, K.]]
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[[Category: Henrick K]]
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[[Category: Endonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:17:02 2008''
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Current revision

THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS

PDB ID 1bao

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