4xnh
From Proteopedia
(Difference between revisions)
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<StructureSection load='4xnh' size='340' side='right'caption='[[4xnh]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4xnh' size='340' side='right'caption='[[4xnh]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4xnh]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4xnh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XNH FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</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=4xnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xnh OCA], [https://pdbe.org/4xnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xnh RCSB], [https://www.ebi.ac.uk/pdbsum/4xnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xnh ProSAT]</span></td></tr> | |
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/NAT1_YEAST NAT1_YEAST] Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome and may present the N termini of nascent polypeptides for acetylation.<ref>PMID:1600941</ref> <ref>PMID:14517307</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Dong | + | [[Category: Dong J]] |
- | [[Category: Wang | + | [[Category: Wang S]] |
- | [[Category: York | + | [[Category: York JD]] |
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Revision as of 17:44, 26 April 2023
Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate
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