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1w42

From Proteopedia

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T. celer L30e R92A variant

Structural highlights

1w42 is a 1 chain structure with sequence from Thermococcus celer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL30E_THECE

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 origin of reduced heat capacity change of unfolding (DeltaC(p)) commonly observed in thermophilic proteins is controversial. The established theory that DeltaC(p) is correlated with change of solvent-accessible surface area cannot account for the large differences in DeltaC(p) observed for thermophilic and mesophilic homologous proteins, which are very similar in structures. We have determined the protein stability curves, which describe the temperature dependency of the free energy change of unfolding, for a thermophilic ribosomal protein L30e from Thermococcus celer, and its mesophilic homologue from yeast. Values of DeltaC(p), obtained by fitting the free energy change of unfolding to the Gibbs-Helmholtz equation, were 5.3 kJ mol(-1) K(-1) and 10.5 kJ mol(-1) K(-1) for T.celer and yeast L30e, respectively. We have created six charge-to-neutral mutants of T.celer L30e. Removal of charges at Glu6, Lys9, and Arg92 decreased the melting temperatures of T.celer L30e by approximately 3-9 degrees C, and the differences in melting temperatures were smaller with increasing concentration of salt. These results suggest that these mutations destabilize T.celer L30e by disrupting favorable electrostatic interactions. To determine whether electrostatic interactions contribute to the reduced DeltaC(p) of the thermophilic protein, we have determined DeltaC(p) for wild-type and mutant T.celer L30e by Gibbs-Helmholtz and by van't Hoff analyses. A concomitant increase in DeltaC(p) was observed for those charge-to-neutral mutants that destabilize T.celer L30e by removing favorable electrostatic interactions. The crystal structures of K9A, E90A, and R92A, were determined, and no structural change was observed. Taken together, our results support the conclusion that electrostatic interactions contribute to the reduced DeltaC(p) of T.celer L30e.

Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e.,Lee CF, Allen MD, Bycroft M, Wong KB J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:15811378^[1]

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

References

↑ Lee CF, Allen MD, Bycroft M, Wong KB. Electrostatic interactions contribute to reduced heat capacity change of unfolding in a thermophilic ribosomal protein l30e. J Mol Biol. 2005 Apr 29;348(2):419-31. PMID:15811378 doi:10.1016/j.jmb.2005.02.052

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w42"

@@ Line 3: / Line 3: @@
 <StructureSection load='1w42' size='340' side='right'caption='[[1w42]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35543 Atcc 35543]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W42 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer Thermococcus celer]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W42 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1go0|1go0]], [[1go1|1go1]], [[1h7m|1h7m]], [[1w3e|1w3e]], [[1w40|1w40]], [[1w41|1w41]]</div></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]] 1.8&#8491;</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=1w42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w42 OCA], [https://pdbe.org/1w42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w42 RCSB], [https://www.ebi.ac.uk/pdbsum/1w42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w42 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/RL30E_THECE RL30E_THECE]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 35543]]
 [[Category: Large Structures]]
-[[Category: Allen, M D]]
+[[Category: Thermococcus celer]]
-[[Category: Bycroft, M]]
+[[Category: Allen MD]]
-[[Category: Chan, S H]]
+[[Category: Bycroft M]]
-[[Category: Lee, C F]]
+[[Category: Chan SH]]
-[[Category: Lee, K M]]
+[[Category: Lee CF]]
-[[Category: Wong, K B]]
+[[Category: Lee KM]]
-[[Category: Electrostatic interaction]]
+[[Category: Wong KB]]
-[[Category: Protein engineering]]
-[[Category: Ribosomal protein]]
-[[Category: Thermostability]]

1w42

From Proteopedia

Current revision

T. celer L30e R92A variant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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