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4HVK

Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.

Summary for 4HVK
Entry DOI10.2210/pdb4hvk/pdb
Related4EB5 4EB7
DescriptorProbable cysteine desulfurase 2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
Functional Keywordstransferase and iscs, transferase
Biological sourceArchaeoglobus fulgidus
Total number of polymer chains1
Total formula weight44194.62
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 citationYamanaka, 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: 23160436
DOI: 10.1039/c2dt32101g
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.43 Å)
Structure validation

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