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1box

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N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS

Structural highlights

1box is a 1 chain structure with sequence from Kitasatospora aureofaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNSA_KITAU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The contribution of hydrogen bonding by peptide groups to the conformational stability of globular proteins was studied. One of the conserved residues in the microbial ribonuclease (RNase) family is an asparagine at position 39 in RNase Sa, 44 in RNase T1, and 58 in RNase Ba (barnase). The amide group of this asparagine is buried and forms two similar intramolecular hydrogen bonds with a neighboring peptide group to anchor a loop on the surface of all three proteins. Thus, it is a good model for the hydrogen bonding of peptide groups. When the conserved asparagine is replaced with alanine, the decrease in the stability of the mutant proteins is 2.2 (Sa), 1.8 (T1), and 2.7 (Ba) kcal/mol. When the conserved asparagine is replaced by aspartate, the stability of the mutant proteins decreases by 1.5 and 1.8 kcal/mol for RNases Sa and T1, respectively, but increases by 0.5 kcal/mol for RNase Ba. When the conserved asparagine was replaced by serine, the stability of the mutant proteins was decreased by 2.3 and 1.7 kcal/mol for RNases Sa and T1, respectively. The structure of the Asn 39 --> Ser mutant of RNase Sa was determined at 1.7 A resolution. There is a significant conformational change near the site of the mutation: (1) the side chain of Ser 39 is oriented differently than that of Asn 39 and forms hydrogen bonds with two conserved water molecules; (2) the peptide bond of Ser 42 changes conformation in the mutant so that the side chain forms three new intramolecular hydrogen bonds with the backbone to replace three hydrogen bonds to water molecules present in the wild-type structure; and (3) the loss of the anchoring hydrogen bonds makes the surface loop more flexible in the mutant than it is in wild-type RNase Sa. The results show that burial and hydrogen bonding of the conserved asparagine make a large contribution to microbial RNase stability and emphasize the importance of structural information in interpreting stability studies of mutant proteins.

Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1.,Hebert EJ, Giletto A, Sevcik J, Urbanikova L, Wilson KS, Dauter Z, Pace CN Biochemistry. 1998 Nov 17;37(46):16192-200. PMID:9819211^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hebert EJ, Giletto A, Sevcik J, Urbanikova L, Wilson KS, Dauter Z, Pace CN. Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1. Biochemistry. 1998 Nov 17;37(46):16192-200. PMID:9819211 doi:10.1021/bi9815243

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1box"

@@ Line 1: / Line 1: @@
 ==N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS==
-<StructureSection load='1box' size='340' side='right' caption='[[1box]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+<StructureSection load='1box' size='340' side='right'caption='[[1box]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1box]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BOX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1box]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BOX FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=1box FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1box OCA], [http://pdbe.org/1box PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1box RCSB], [http://www.ebi.ac.uk/pdbsum/1box PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1box ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1box FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1box OCA], [https://pdbe.org/1box PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1box RCSB], [https://www.ebi.ac.uk/pdbsum/1box PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1box ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RNSA_KITAU RNSA_KITAU]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/1box_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/1box_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 30: @@
 ==See Also==
-*[[Ribonuclease|Ribonuclease]]
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-*[[Temp|Temp]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Dauter, Z]]
+[[Category: Kitasatospora aureofaciens]]
-[[Category: Giletto, A]]
+[[Category: Large Structures]]
-[[Category: Hebert, E J]]
+[[Category: Dauter Z]]
-[[Category: Pace, C N]]
+[[Category: Giletto A]]
-[[Category: Sevcik, J]]
+[[Category: Hebert EJ]]
-[[Category: Urbanikova, L]]
+[[Category: Pace CN]]
-[[Category: Wilson, K S]]
+[[Category: Sevcik J]]
-[[Category: Hydrolase]]
+[[Category: Urbanikova L]]
-[[Category: Mutant]]
+[[Category: Wilson KS]]
-[[Category: Ribonuclease]]

1box

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Current revision

N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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