2ld4: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ld4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld4 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ld4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ld4 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CPIN1_HUMAN CPIN1_HUMAN]] May be required for the maturation of extramitochondrial Fe/S proteins (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity).[HAMAP-Rule:MF_03115] | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 20:50, 25 December 2014
Solution structure of the N-terminal domain of human anamorsinSolution structure of the N-terminal domain of human anamorsin
Structural highlights
Function[CPIN1_HUMAN] May be required for the maturation of extramitochondrial Fe/S proteins (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity).[HAMAP-Rule:MF_03115] Publication Abstract from PubMedHuman 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. Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery.,Banci L, Bertini I, Ciofi-Baffoni S, Boscaro F, Chatzi A, Mikolajczyk M, Tokatlidis K, Winkelmann J Chem Biol. 2011 Jun 24;18(6):794-804. PMID:21700214[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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