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1bri

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(New page: 200px<br /><applet load="1bri" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bri, resolution 1.9&Aring;" /> '''BARNASE MUTANT WITH I...)
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[[Image:1bri.gif|left|200px]]<br /><applet load="1bri" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bri, resolution 1.9&Aring;" />
 
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'''BARNASE MUTANT WITH ILE 76 REPLACED BY ALA'''<br />
 
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==Overview==
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==BARNASE MUTANT WITH ILE 76 REPLACED BY ALA==
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We have solved the 2.0-A resolution crystal structures of four, cavity-creating Ile/Leu--&gt;Ala mutations in the hydrophobic core of barnase, and compare and contrast the structural responses to mutation with those, found for Leu--&gt;Ala mutations in T4 lysozyme. First, there are, rearrangements of structure of barnase that cause the cavities to collapse, partly, and there is an approximately linear relationship between the, changes in stability and the volume of the cavity similar to that found, for the mutants of T4 lysozyme. Second, although it is currently accepted, that hydrophobic cavities formed on the mutation of large hydrophobic side, chains to smaller ones are not occupied by water molecules, we found a, buried water molecule in the crystal structure of the barnase mutant, Ile76--&gt;Ala. A single hydrogen bond is formed between the water molecule, and a polar atom, the carbonyl oxygen of Phe7, in the hydrophobic cavity, that is formed on mutation. A survey of hydrophobic cavities produced by, similar mutations in different proteins reveals that they all contain a, proportion of polar atoms in their linings. The availability of such polar, sites has implications for understanding folding pathways because a, solvated core is presumed present in the transition state for folding and, unfolding. Notably, the hydrogen bond between the cavity-water and the, carbonyl group of Phe7 is also a marked early feature of very recent, molecular dynamics simulations of barnase denaturation [Caflisch, A., &amp;, Karplus, M. (1995) J. Mol. Biol. 252, 672-708]. It is possible that, cavities engineered into the hydrophobic cores of other proteins may, contain water molecules, even though they cannot be detected by, crystallographic analysis.
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<StructureSection load='1bri' size='340' side='right'caption='[[1bri]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bri]] 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=1BRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRI 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">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</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=1bri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bri OCA], [https://pdbe.org/1bri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bri RCSB], [https://www.ebi.ac.uk/pdbsum/1bri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bri 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/br/1bri_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=1bri ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRI OCA].
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*[[Barnase 3D structures|Barnase 3D structures]]
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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==Reference==
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__TOC__
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Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities., Buckle AM, Cramer P, Fersht AR, Biochemistry. 1996 Apr 9;35(14):4298-305. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8605178 8605178]
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</StructureSection>
[[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: Buckle, A.]]
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[[Category: Buckle A]]
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[[Category: Cramer, P.C.]]
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[[Category: Cramer PC]]
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[[Category: Fersht, A.]]
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[[Category: Fersht A]]
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[[Category: alpha/beta protein alpha/beta protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:51:36 2007''
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Current revision

BARNASE MUTANT WITH ILE 76 REPLACED BY ALA

PDB ID 1bri

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