2O5U

Crystal structure of the PA5185 protein from Pseudomonas Aeruginosa strain PAO1- orthorhombic form (C222).

Summary for 2O5U

• Entry DOI: 10.2210/pdb2o5u/pdb
• Related: 2AV9
• Descriptor: Thioesterase (2 entities in total)
• Functional Keywords: putative thioesterese, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 3
• Total formula weight: 49654.96

Authors

Chruszcz, M.,Wang, S.,Evdokimova, E.,Koclega, K.D.,Kudritska, M.,Savchenko, A.,Edwards, A.,Minor, W. (deposition date: 2006-12-06, release date: 2007-12-18, Last modification date: 2023-08-30)

Primary citation

Chruszcz, M.,Zimmerman, M.D.,Wang, S.,Koclega, K.D.,Zheng, H.,Evdokimova, E.,Kudritska, M.,Cymborowski, M.,Savchenko, A.,Edwards, A.,Minor, W.
Function-biased choice of additives for optimization of protein crystallization - the case of the putative thioesterase PA5185 from Pseudomonas aeruginosa PAO1.
Cryst.Growth Des., 8:4054-4061, 2008

PubMed Abstract: The crystal structure of PA5185, a putative thioesterase from Pseudomonas aeruginosa strain PAO1, was solved using multi-wavelength anomalous diffraction to 2.4 Å. Analysis of the structure and information about the putative function of the protein were used to optimize crystallization conditions. The crystal growth was optimized by applying additives with chemical similarity to a fragment of a putative PA5185 substrate (CoA or its derivative). Using new crystallization conditions containing this function-biased set of additives, several new crystal forms were produced and structures of three of them (in three different space groups) were determined. One of the new crystal forms had an improved resolution limit of 1.9 Å, and another displayed an alternative conformation of the highly-conserved loop containing Asn26, which could play a physiological role. Surprisingly, none of the additives were ordered in the crystal structures. Application of function-biased additives could be used as a standard optimization protocol for producing improved diffraction, or new crystal forms, which may lead to better understanding of the biological functions of proteins.

PubMed: 19898606
DOI: 10.1021/cg800430f

Experimental method

X-RAY DIFFRACTION (1.91 Å)