5JJC
Crystal Structure of double mutant (Q96A-Y125A) O-Acetyl Serine Sulfhydralase from Brucella abortus
Summary for 5JJC
| Entry DOI | 10.2210/pdb5jjc/pdb |
| Related | 5JIS |
| Descriptor | Cysteine synthase (2 entities in total) |
| Functional Keywords | cysteine synthase, transferase |
| Biological source | Brucella abortus S19 |
| Total number of polymer chains | 4 |
| Total formula weight | 147273.83 |
| Authors | Dharavath, S.,Gourinath, S. (deposition date: 2016-04-23, release date: 2017-04-05, Last modification date: 2023-11-15) |
| Primary citation | Dharavath, S.,Raj, I.,Gourinath, S. Structure-based mutational studies of O-acetylserine sulfhydrylase reveal the reason for the loss of cysteine synthase complex formation in Brucella abortus Biochem. J., 474:1221-1239, 2017 Cited by PubMed Abstract: Cysteine biosynthesis takes place via a two-step pathway in bacteria, fungi, plants and protozoan parasites, but not in humans, and hence, the machinery of cysteine biosynthesis is an opportune target for therapeutics. The decameric cysteine synthase complex (CSC) is formed when the C-terminal tail of serine acetyltransferase (SAT) binds in the active site of -acetylserine sulfydrylase (OASS), playing a role in the regulation of this pathway. Here, we show that OASS from (BaOASS) does not interact with its cognate SAT C-terminal tail. Crystal structures of native BaOASS showed that residues Gln96 and Tyr125 occupy the active-site pocket and interfere with the entry of the SAT C-terminal tail. The BaOASS (Q96A-Y125A) mutant showed relatively strong binding ( = 32.4 μM) to BaSAT C-terminal peptides in comparison with native BaOASS. The mutant structure looks similar except that the active-site pocket has enough space to bind the SAT C-terminal end. Surface plasmon resonance results showed a relatively strong (7.3 μM ) interaction between BaSAT and the BaOASS (Q96A-Y125A), but no interaction with native BaOASS. Taken together, our observations suggest that the CSC does not form in . PubMed: 28126739DOI: 10.1042/BCJ20161062 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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