Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1

Journal of Molecular Biology
Takashi NakamuraKazuhiko Ishikawa

Abstract

L-Cysteine is synthesized from O-acetyl-L-serine (OAS) and sulfide by O-acetylserine sulfhydrylase (OASS; EC 2.5.1.47) in plants and bacteria. O-phosphoserine sulfhydrylase (OPSS; EC 2.5.1.65) is a novel enzyme from the hyperthermophilic aerobic archaeon Aeropyrum pernix K1 (2003). OPSS can use OAS or O-phospho-L-serine (OPS) to synthesize L-cysteine. To elucidate the mechanism of the substrate specificity of OPSS, we analyzed three-dimensional structures of the active site of the enzyme. The active-site lysine (K127) of OPSS forms an internal Schiff base with pyridoxal 5'-phosphate. Therefore, crystals of the complexes formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with either OPS or OAS were prepared and examined by X-ray diffraction analysis. In contrast to that observed for OASS, no significant difference was seen in the overall structure between the free and complexed forms of OPSS. The side chains of T152, S153, and Q224 interacted with the carboxylate of the substrates, as a previous study has suggested. The side chain of R297 has been proposed to recognize the phosphate group of OPS. Surprisingly, however, the position of R297 was significantly unchanged in the complex of the OPSS K12...Continue Reading

References

Sep 19, 2000·Bioscience, Biotechnology, and Biochemistry·K MinoK Nakanishi
Jan 31, 2003·Proteins·Simon C LovellDavid C Richardson
Mar 20, 2003·Journal of Bacteriology·Koshiki Mino, Kazuhiko Ishikawa
Apr 10, 2004·The Journal of Biological Chemistry·Wael M Rabeh, Paul F Cook
Sep 1, 1994·Acta Crystallographica. Section D, Biological Crystallography·UNKNOWN Collaborative Computational Project, Number 4
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·Paul Emsley, Kevin Cowtan
Jun 15, 2005·Biochemistry·Michael T ClausGeorg E Schulz
Mar 21, 2006·Protein Expression and Purification·Chunhui ZhaoKazuhiro Nakanishi
Jun 1, 2006·The Journal of Biological Chemistry·Gareth D WestropGraham H Coombs
May 17, 2007·Current Medicinal Chemistry·Alessio AmadasiAndrea Mozzarelli
Nov 1, 2007·Infectious Disorders Drug Targets·Devayani P BhaveKate S Carroll
Nov 26, 2009·Journal of Medicinal Chemistry·Enea SalsiAndrea Mozzarelli
Oct 6, 2010·Journal of Structural and Functional Genomics·Alexander K GoroncyShigeyuki Yokoyama

❮ Previous
Next ❯

Citations

Oct 30, 2013·PloS One·Francesca SpyrakisAndrea Mozzarelli
Mar 21, 2013·Current Opinion in Structural Biology·Joseph M Jez, Sanghamitra Dey
Mar 18, 2015·Bioscience, Biotechnology, and Biochemistry·Takashi NakamuraKazuhiko Ishikawa
Jul 6, 2016·Extremophiles : Life Under Extreme Conditions·Emi TakedaTakashi Nakamura
Mar 3, 2019·Journal of Experimental Botany·Joseph M Jez
Feb 11, 2021·Journal of Bioscience and Bioengineering·Emi TakedaTakashi Nakamura
Sep 4, 2014·Biochemistry·Florian BuschReinhard Sterner

❮ Previous
Next ❯

Related Concepts

Related Feeds

Amoebiasis

Amoebiasis, infection by the protozoan parasite Entamoeba histolytica, remains a global health problem, despite the availability of effective treatment. Here is the latest research.