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==Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Leu-Ala-Ala-Arg peptide== | |||
<StructureSection load='6a0h' size='340' side='right'caption='[[6a0h]], [[Resolution|resolution]] 3.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6a0h]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A0H FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
[[Category: | <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=6a0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a0h OCA], [http://pdbe.org/6a0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a0h RCSB], [http://www.ebi.ac.uk/pdbsum/6a0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a0h ProSAT]</span></td></tr> | ||
[[Category: Park, J | </table> | ||
[[Category: | == Function == | ||
[[http://www.uniprot.org/uniprot/NTAN1_HUMAN NTAN1_HUMAN]] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.<ref>PMID:21375249</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Han, B W]] | |||
[[Category: Park, J S]] | |||
[[Category: Amidohydrolase]] | |||
[[Category: Complex]] | |||
[[Category: Hydrolase]] | |||
Revision as of 18:01, 11 December 2019
Crystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Leu-Ala-Ala-Arg peptideCrystal structure of human protein N-terminal asparagine amidohydrolase (NTAN1) C75S mutant with Asn-Leu-Ala-Ala-Arg peptide
Structural highlights
Function[NTAN1_HUMAN] N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.[1] References
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