2LD4

Solution structure of the N-terminal domain of human anamorsin

Summary for 2LD4

• Entry DOI: 10.2210/pdb2ld4/pdb
• NMR Information: BMRB: 17646
• Descriptor: Anamorsin (1 entity in total)
• Functional Keywords: methyltransferase-like fold, alpha/beta fold, iron-sulfur protein biogenesis, apoptosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18931.54

Authors

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Boscaro, F.,Chatzi, A.,Mikolajczyk, M.,Tokatlidis, K.,Winkelmann, J. (deposition date: 2011-05-13, release date: 2011-07-13, Last modification date: 2024-05-01)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Boscaro, F.,Chatzi, A.,Mikolajczyk, M.,Tokatlidis, K.,Winkelmann, J.
Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery.
Chem.Biol., 18:794-804, 2011

PubMed Abstract: Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.

PubMed: 21700214
DOI: 10.1016/j.chembiol.2011.03.015

Experimental method

SOLUTION NMR