3aa9 | pdb_00003aa9

Crystal Structure Analysis of the Mutant CutA1 (E61V) from E. coli

spinqualitylabelsall models 3aa9, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3aa9 is a 3 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CUTA_ECOLI Involved in resistance toward heavy metals. 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CutA1 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA