4xpd: Difference between revisions
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==Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate== | |||
<StructureSection load='4xpd' size='340' side='right' caption='[[4xpd]], [[Resolution|resolution]] 2.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xpd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=CMC:CARBOXYMETHYL+COENZYME+*A'>CMC</scene>, <scene name='pdbligand=G4P:GUANOSINE-5,3-TETRAPHOSPHATE'>G4P</scene></td></tr> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xnh|4xnh]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_alpha-N-acetyltransferase Peptide alpha-N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.88 2.3.1.88] </span></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=4xpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpd OCA], [http://pdbe.org/4xpd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xpd RCSB], [http://www.ebi.ac.uk/pdbsum/4xpd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xpd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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> [[http://www.uniprot.org/uniprot/NAT5_YEAST NAT5_YEAST]] Non-essential 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. [[http://www.uniprot.org/uniprot/ARD1_YEAST ARD1_YEAST]] 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.<ref>PMID:1600941</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Peptide alpha-N-acetyltransferase]] | |||
[[Category: Dong, J]] | |||
[[Category: Wang, S]] | |||
[[Category: York, J D]] | |||
[[Category: Bisubstrate]] | |||
[[Category: N-terminal acetyltransferase]] | |||
[[Category: Nate]] | |||
[[Category: Ppgpp]] | |||
[[Category: Transferase]] | |||
Revision as of 15:24, 26 July 2016
Crystal structure of yeast N-terminal acetyltransferase NatE (ppGpp) in complex with a bisubstrate
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