3aa9: Difference between revisions
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< | ==Crystal Structure Analysis of the Mutant CutA1 (E61V) from E. coli== | ||
<StructureSection load='3aa9' size='340' side='right'caption='[[3aa9]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3aa9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AA9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=3aa9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aa9 OCA], [https://pdbe.org/3aa9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aa9 RCSB], [https://www.ebi.ac.uk/pdbsum/3aa9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aa9 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CUTA_ECOLI CUTA_ECOLI] Involved in resistance toward heavy metals.<ref>PMID:7623666</ref> | |||
== 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/aa/3aa9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=3aa9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To enhance the heat stability of the CutA1 protein from Escherichia coli (EcCutA1) so that it has comparable stability to CutA1 from Pyrococcus horikoshii with a denaturation temperature (T(d)) of 150( degrees )C, we used the Stability Profile of Mutant Protein (SPMP) to examine the structure-sequence (3D-1D) compatibility between the conformation of EcCutA1 and its native sequence (J. Mol. Biol., 248, 733-738, (1995)). We identified seven residues in EcCutA1 that were incompatible in terms of dihedral angles and hydrophobicity. These residues were replaced with appropriate amino acids, and the mutant proteins were evaluated for changes in stability by DSC and denaturant denaturation. The mutations that were introduced at five out of the seven positions improved the stability of EcCutA1. The T(d) values of single (S11A) and triple (S11V/E61V/Q73V) mutants improved by 16.5 and 26.6( degrees )C, respectively, compared to that of the wild-type protein (89.9( degrees )C). These analyses showed that (1) the stability of EcCutA1 is remarkably improved by slight substitutions, even though the stability of the wild-type protein is considerably high, (2) remarkable improvements in the stability can be quantitatively explained based on the newly solved native structure, and (3) SPMP is a powerful tool to examine substitutions that improve protein stability. | |||
Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design.,Matsuura Y, Ota M, Tanaka T, Takehira M, Ogasahara K, Bagautdinov B, Kunishima N, Yutani K J Biochem. 2010 Jul 16. PMID:20639520<ref>PMID:20639520</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3aa9" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CutA1 3D structures|CutA1 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Escherichia coli K-12]] | ||
[[ | [[Category: Large Structures]] | ||
[[Category: Bagautdinov B]] | |||
== | [[Category: Kunishima N]] | ||
< | [[Category: Matsuura Y]] | ||
[[Category: Escherichia coli]] | [[Category: Tanaka T]] | ||
[[Category: Bagautdinov | [[Category: Yutani K]] | ||
[[Category: Kunishima | |||
[[Category: Matsuura | |||
[[Category: Tanaka | |||
[[Category: Yutani | |||
Latest revision as of 17:16, 1 November 2023
Crystal Structure Analysis of the Mutant CutA1 (E61V) from E. coliCrystal Structure Analysis of the Mutant CutA1 (E61V) from E. coli
Structural highlights
FunctionCUTA_ECOLI Involved in resistance toward heavy metals.[1] 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 PubMedTo enhance the heat stability of the CutA1 protein from Escherichia coli (EcCutA1) so that it has comparable stability to CutA1 from Pyrococcus horikoshii with a denaturation temperature (T(d)) of 150( degrees )C, we used the Stability Profile of Mutant Protein (SPMP) to examine the structure-sequence (3D-1D) compatibility between the conformation of EcCutA1 and its native sequence (J. Mol. Biol., 248, 733-738, (1995)). We identified seven residues in EcCutA1 that were incompatible in terms of dihedral angles and hydrophobicity. These residues were replaced with appropriate amino acids, and the mutant proteins were evaluated for changes in stability by DSC and denaturant denaturation. The mutations that were introduced at five out of the seven positions improved the stability of EcCutA1. The T(d) values of single (S11A) and triple (S11V/E61V/Q73V) mutants improved by 16.5 and 26.6( degrees )C, respectively, compared to that of the wild-type protein (89.9( degrees )C). These analyses showed that (1) the stability of EcCutA1 is remarkably improved by slight substitutions, even though the stability of the wild-type protein is considerably high, (2) remarkable improvements in the stability can be quantitatively explained based on the newly solved native structure, and (3) SPMP is a powerful tool to examine substitutions that improve protein stability. Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design.,Matsuura Y, Ota M, Tanaka T, Takehira M, Ogasahara K, Bagautdinov B, Kunishima N, Yutani K J Biochem. 2010 Jul 16. PMID:20639520[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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