4m7r: Difference between revisions
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==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=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m7r]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | |||
<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 Homo sapiens])</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://www.rcsb.org/pdb/explore.do?structureId=4m7r RCSB], [http://www.ebi.ac.uk/pdbsum/4m7r PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Liu, Z J | [[Category: Liu, Z J]] | ||
[[Category: Song, G | [[Category: Song, G]] | ||
[[Category: Apoptosis]] | [[Category: Apoptosis]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 14:54, 21 December 2014
Crystal structure of the N-terminal methyltransferase-like domain of anamorsin
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