4m7r

<StructureSection load='4m7r' size='340' side='right'caption='[[4m7r]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[4m7r]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M7R FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=4m7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m7r OCA], [https://pdbe.org/4m7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m7r RCSB], [https://www.ebi.ac.uk/pdbsum/4m7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m7r ProSAT]</span></td></tr>

== 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]

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== Publication Abstract from PubMed ==

Anamorsin is a recently identified molecule that inhibits apoptosis during hematopoiesis. It contains an N-terminal methyltransferase-like domain and a C-terminal Fe-S cluster motif. Not much is known about the function of the protein. To better understand the function of anamorsin, we have solved the crystal structure of the N-terminal domain at 1.8 A resolution. Although the overall structure resembles a typical S-adenosylmethionine (SAM) dependent methyltransferase fold, it lacks one alpha-helix and one beta-strand. As a result, the N-terminal domain as well as the full-length anamorsin did not show S-adenosyl-L-methionine (AdoMet) dependent methyltransferase activity. Structural comparisons with known AdoMet dependent methyltransferases reveals subtle differences in the SAM binding pocket that preclude the N-terminal domain from binding to AdoMet. The N-terminal methyltransferase-like domain of anamorsin probably functions as a structural scaffold to inhibit methyl transfers by out-competing other AdoMet dependant methyltransferases or acts as bait for protein-protein interactions. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.

Crystal structure of the N-terminal methyltransferase-like domain of anamorsin.,Song G, Cheng C, Li Y, Shaw N, Xiao Z, Liu ZJ Proteins. 2013 Oct 9. doi: 10.1002/prot.24443. PMID:24123282<ref>PMID:24123282</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4m7r" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Liu, Z J]]

[[Category: Song, G]]

[[Category: Rossmann fold]]