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==Crystal structure analysis of Streptomyces aureofaciens ribonuclease Sa Y51F mutant== | ==Crystal structure analysis of Streptomyces aureofaciens ribonuclease Sa Y51F mutant== | ||
<StructureSection load='4j5k' size='340' side='right' caption='[[4j5k]], [[Resolution|resolution]] 1.23Å' scene=''> | <StructureSection load='4j5k' size='340' side='right' caption='[[4j5k]], [[Resolution|resolution]] 1.23Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sar|1sar]], [[1lni|1lni]], [[1gmp|1gmp]], [[1axy|1axy]], [[1t2i|1t2i]], [[1rge|1rge]], [[1rgf|1rgf]], [[1rgg|1rgg]], [[1rgh|1rgh]], [[1rsn|1rsn]], [[2sar|2sar]], [[4j5g|4j5g]], [[4gho|4gho]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sar|1sar]], [[1lni|1lni]], [[1gmp|1gmp]], [[1axy|1axy]], [[1t2i|1t2i]], [[1rge|1rge]], [[1rgf|1rgf]], [[1rgg|1rgg]], [[1rgh|1rgh]], [[1rsn|1rsn]], [[2sar|2sar]], [[4j5g|4j5g]], [[4gho|4gho]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j5k RCSB], [http://www.ebi.ac.uk/pdbsum/4j5k PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5k OCA], [http://pdbe.org/4j5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5k RCSB], [http://www.ebi.ac.uk/pdbsum/4j5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4j5k" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ribonuclease|Ribonuclease]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:22, 11 August 2016
Crystal structure analysis of Streptomyces aureofaciens ribonuclease Sa Y51F mutantCrystal structure analysis of Streptomyces aureofaciens ribonuclease Sa Y51F mutant
Structural highlights
Publication Abstract from PubMedOur goal was to gain a better understanding of the contribution of the burial of polar groups and their hydrogen bonds to the conformational stability of proteins. We measured the change in stability, Delta(DeltaG), for a series of hydrogen bonding mutants in four proteins: villin headpiece subdomain (VHP) containing 36 residues, a surface protein from Borrelia burgdorferi (VlsE) containing 341 residues, and two proteins previously studied in our laboratory, ribonucleases Sa (RNase Sa) and T1 (RNase T1). Crystal structures were determined for three of the hydrogen bonding mutants of RNase Sa: S24A, Y51F, and T95A. The structures are very similar to wild type RNase Sa and the hydrogen bonding partners form intermolecular hydrogen bonds to water in all three mutants. We compare our results with previous studies of similar mutants in other proteins and reach the following conclusions. (1) Hydrogen bonds contribute favorably to protein stability. (2) The contribution of hydrogen bonds to protein stability is strongly context dependent. (3) Hydrogen bonds by side chains and peptide groups make similar contributions to protein stability. (4) Polar group burial can make a favorable contribution to protein stability even if the polar groups are not hydrogen bonded. (5) The contribution of hydrogen bonds to protein stability is similar for VHP, a small protein, and VlsE, a large protein. Contribution of hydrogen bonds to protein stability.,Pace CN, Fu H, Lee Fryar K, Landua J, Trevino SR, Schell D, Thurlkill RL, Imura S, Scholtz JM, Gajiwala K, Sevcik J, Urbanikova L, Myers JK, Takano K, Hebert EJ, Shirley BA, Grimsley GR Protein Sci. 2014 May;23(5):652-61. doi: 10.1002/pro.2449. Epub 2014 Mar 25. PMID:24591301[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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