4GHO

Crystal Structure Analysis of Streptomyces aureofaciens Ribonuclease S24A mutant

Summary for 4GHO

• Entry DOI: 10.2210/pdb4gho/pdb
• Related: 1AX7 1BOX 1GMP 1I70 1I8V 1LNI 1RGE 1RGF 1RGG 1RGH 1RSN 1SAR 1T2H 1T2I 1ZGX 2SAR 4J5G 4J5K
• Descriptor: Guanyl-specific ribonuclease Sa, SULFATE ION (3 entities in total)
• Functional Keywords: structural genomics, enzyme function initiative, alpha helix, three-stranded beta sheet, hydrolase
• Biological source: Streptomyces aureofaciens
• Cellular location: Secreted: P05798
• Total number of polymer chains: 2
• Total formula weight: 21229.05

Authors

Sevcik, J.,Urbanikova, L. (deposition date: 2012-08-08, release date: 2013-08-14, Last modification date: 2024-11-06)

Primary citation

Pace, C.N.,Fu, H.,Fryar, K.L.,Landua, J.,Trevino, S.R.,Schell, D.,Thurlkill, R.L.,Imura, S.,Scholtz, J.M.,Gajiwala, K.,Sevcik, J.,Urbanikova, L.,Myers, J.K.,Takano, K.,Hebert, E.J.,Shirley, B.A.,Grimsley, G.R.
Contribution of hydrogen bonds to protein stability
Protein Sci., 23:652-661, 2014

PubMed Abstract: Our 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, Δ(ΔG), 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.

PubMed: 24591301
DOI: 10.1002/pro.2449

Experimental method

X-RAY DIFFRACTION (1.1 Å)