2RHS

PheRS from Staphylococcus haemolyticus- rational protein engineering and inhibitor studies

Summary for 2RHS

• Entry DOI: 10.2210/pdb2rhs/pdb
• Related: 2RHQ
• Descriptor: Phenylalanyl-tRNA synthetase alpha chain, Phenylalanyl-tRNA synthetase beta chain, 1-{3-[(4-pyridin-2-ylpiperazin-1-yl)sulfonyl]phenyl}-3-(1,3-thiazol-2-yl)urea, ... (6 entities in total)
• Functional Keywords: heterotetramer, phenylalanine, trna, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, magnesium, metal-binding, nucleotide-binding, protein biosynthesis, rna-binding, trna-binding
• Biological source: Staphylococcus haemolyticus; More
• Cellular location: Cytoplasm : Q4L5E3 Q4L5E4
• Total number of polymer chains: 4
• Total formula weight: 245446.04

Authors

Evdokimov, A.G.,Mekel, M. (deposition date: 2007-10-09, release date: 2007-11-06, Last modification date: 2024-02-21)

Primary citation

Evdokimov, A.G.,Mekel, M.,Hutchings, K.,Narasimhan, L.,Holler, T.,McGrath, T.,Beattie, B.,Fauman, E.,Yan, C.,Heaslet, H.,Walter, R.,Finzel, B.,Ohren, J.,McConnell, P.,Braden, T.,Sun, F.,Spessard, C.,Banotai, C.,Al-Kassim, L.,Ma, W.,Wengender, P.,Kole, D.,Garceau, N.,Toogood, P.,Liu, J.
Rational protein engineering in action: the first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus.
J.Struct.Biol., 162:152-169, 2008

PubMed Abstract: In this article, we describe for the first time the high-resolution crystal structure of a phenylalanine tRNA synthetase from the pathogenic bacterium Staphylococcus haemolyticus. We demonstrate the subtle yet important structural differences between this enzyme and the previously described Thermus thermophilus ortholog. We also explain the structure-activity relationship of several recently reported inhibitors. The native enzyme crystals were of poor quality--they only diffracted X-rays to 3-5A resolution. Therefore, we have executed a rational surface mutagenesis strategy that has yielded crystals of this 2300-amino acid multidomain protein, diffracting to 2A or better. This methodology is discussed and contrasted with the more traditional domain truncation approach.

PubMed: 18086534
DOI: 10.1016/j.jsb.2007.11.002

Experimental method

X-RAY DIFFRACTION (2.2 Å)