2ld4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Solution structure of the N-terminal domain of human anamorsin==
==Solution structure of the N-terminal domain of human anamorsin==
<StructureSection load='2ld4' size='340' side='right'caption='[[2ld4]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
<StructureSection load='2ld4' size='340' side='right'caption='[[2ld4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ld4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2ld4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LD4 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIAPIN1, CUA001, PRO0915 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld4 OCA], [https://pdbe.org/2ld4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld4 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ld4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ld4 OCA], [https://pdbe.org/2ld4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ld4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ld4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ld4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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]  
[https://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]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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<ref>PMID:21700214</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ld4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Banci, L]]
[[Category: Banci L]]
[[Category: Bertini, I]]
[[Category: Bertini I]]
[[Category: Boscaro, F]]
[[Category: Boscaro F]]
[[Category: Chatzi, A]]
[[Category: Chatzi A]]
[[Category: Ciofi-Baffoni, S]]
[[Category: Ciofi-Baffoni S]]
[[Category: Mikolajczyk, M]]
[[Category: Mikolajczyk M]]
[[Category: Tokatlidis, K]]
[[Category: Tokatlidis K]]
[[Category: Winkelmann, J]]
[[Category: Winkelmann J]]
[[Category: Alpha/beta fold]]
[[Category: Apoptosis]]
[[Category: Iron-sulfur protein biogenesis]]
[[Category: Methyltransferase-like fold]]

Latest revision as of 09:55, 1 May 2024

Solution structure of the N-terminal domain of human anamorsinSolution structure of the N-terminal domain of human anamorsin

Structural highlights

2ld4 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2ld4&oldid=4136299"