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| | ==Crystal structure of the N-terminal methyltransferase-like domain of anamorsin== | | ==Crystal structure of the N-terminal methyltransferase-like domain of anamorsin== |
| - | <StructureSection load='4m7r' size='340' side='right' caption='[[4m7r]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4m7r' size='340' side='right'caption='[[4m7r]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m7r]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M7R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m7r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.801Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CIAPIN1, CUA001, PRO0915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m7r OCA], [http://pdbe.org/4m7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m7r RCSB], [http://www.ebi.ac.uk/pdbsum/4m7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m7r 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=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> |
| | </table> | | </table> |
| | == Function == | | == 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] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Liu, Z J]] | + | [[Category: Large Structures]] |
| - | [[Category: Song, G]] | + | [[Category: Liu Z-J]] |
| - | [[Category: Apoptosis]] | + | [[Category: Song G]] |
| - | [[Category: Rossmann fold]]
| + | |
| 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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Song G, Cheng C, Li Y, Shaw N, Xiao Z, Liu ZJ. Crystal structure of the N-terminal methyltransferase-like domain of anamorsin. Proteins. 2013 Oct 9. doi: 10.1002/prot.24443. PMID:24123282 doi:http://dx.doi.org/10.1002/prot.24443
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