4HVK
Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.
Summary for 4HVK
| Entry DOI | 10.2210/pdb4hvk/pdb |
| Related | 4EB5 4EB7 |
| Descriptor | Probable cysteine desulfurase 2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | transferase and iscs, transferase |
| Biological source | Archaeoglobus fulgidus |
| Total number of polymer chains | 1 |
| Total formula weight | 44194.62 |
| Authors | Yamanaka, Y.,Zeppieri, L.,Nicolet, Y.,Marinoni, E.N.,de Oliveira, J.S.,Masafumi, O.,Dean, D.R.,Fontecilla-Camps, J.C. (deposition date: 2012-11-06, release date: 2012-12-05, Last modification date: 2024-02-28) |
| Primary citation | Yamanaka, Y.,Zeppieri, L.,Nicolet, Y.,Marinoni, E.N.,de Oliveira, J.S.,Odaka, M.,Dean, D.R.,Fontecilla-Camps, J.C. Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus. Dalton Trans, 42:3092-3099, 2013 Cited by PubMed Abstract: L-Cysteine desulfurase IscS and scaffold IscU proteins are universally involved in Fe/S cluster synthesis. The Archaeoglobus fulgidus (Af) genome encodes proteins having a high degree of primary structure similarity to IscS and IscU from other organisms. However, AfIscS is unusual because it lacks the active site lysine residue that normally forms an internal Schiff base with pyridoxal-phosphate (PLP) and serves as a base during catalysis. Our as-isolated recombinant AfIscS contains pyridoxamine phosphate (PMP) instead of the expected PLP and lacks desulfurase activity. We have solved its structure to 1.43 Å resolution and found that PMP binds non-covalently at the PLP site of the enzyme and displays significant disorder. However, the previously reported structure of recombinant Af(IscU-D35A-IscS)(2) contains an in vivo generated [Fe(2)S(2)] species within AfIscU and the question arises as to how its sulfides were generated. Here, we report that adding PLP to AfIscS produces an enzyme that displays in vitro L-cysteine desulfurase activity mediating the synthesis of a stable holo Af(IscU-D35A-IscS) complex. PubMed: 23160436DOI: 10.1039/c2dt32101g PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.43 Å) |
Structure validation
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