4kvm: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4kvm' size='340' side='right'caption='[[4kvm]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='4kvm' size='340' side='right'caption='[[4kvm]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4kvm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4kvm]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KVM FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1XE:[5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)furan-2-yl]methyl+(3R)-4-{[3-({(E)-2-[(2,2-dihydroxyethyl)sulfanyl]ethenyl}amino)-3-oxopropyl]amino}-3-hydroxy-2,2-dimethyl-4-oxobutyl+dihydrogen+diphosphate'>1XE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.597Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1XE:[5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)furan-2-yl]methyl+(3R)-4-{[3-({(E)-2-[(2,2-dihydroxyethyl)sulfanyl]ethenyl}amino)-3-oxopropyl]amino}-3-hydroxy-2,2-dimethyl-4-oxobutyl+dihydrogen+diphosphate'>1XE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4kvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kvm OCA], [https://pdbe.org/4kvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kvm RCSB], [https://www.ebi.ac.uk/pdbsum/4kvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kvm 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=4kvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kvm OCA], [https://pdbe.org/4kvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kvm RCSB], [https://www.ebi.ac.uk/pdbsum/4kvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kvm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NAT1_SCHPO NAT1_SCHPO] 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 (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Schizosaccharomyces pombe 972h-]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Liszczak GP]] | ||
[[Category: | [[Category: Marmorstein RQ]] | ||
Revision as of 00:39, 29 June 2023
The NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analogThe NatA (Naa10p/Naa15p) amino-terminal acetyltransferase complex bound to a bisubstrate analog
Structural highlights
FunctionNAT1_SCHPO 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 (By similarity). Publication Abstract from PubMedN-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstrate peptide-CoA-conjugate inhibitor, as well as the structure of the uncomplexed Naa10p catalytic subunit. The NatA-Naa15p auxiliary subunit contains 13 tetratricopeptide motifs and adopts a ring-like topology that wraps around the NatA-Naa10p subunit, an interaction that alters the Naa10p active site for substrate-specific acetylation. These studies have implications for understanding the mechanistic details of other NAT complexes and how regulatory subunits modulate the activity of the broader family of protein acetyltransferases. Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.,Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R Nat Struct Mol Biol. 2013 Aug 4. doi: 10.1038/nsmb.2636. PMID:23912279[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||