4xnh

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'''Unreleased structure'''
 
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The entry 4xnh is ON HOLD until Jul 20 2017
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==Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate==
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<StructureSection load='4xnh' size='340' side='right' caption='[[4xnh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4xnh]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XNH FirstGlance]. <br>
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Description:
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</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=I6P:INOSITOL+1,2,3,4,5,6-HEXAKISPHOSPHATE'>I6P</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xpd|4xpd]]</td></tr>
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<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>
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<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=4xnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xnh OCA], [http://pdbe.org/4xnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xnh RCSB], [http://www.ebi.ac.uk/pdbsum/4xnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xnh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Peptide alpha-N-acetyltransferase]]
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[[Category: Dong, J]]
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[[Category: Wang, S]]
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[[Category: York, J D]]
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[[Category: Bisubstrate]]
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[[Category: Inositol hexaxisphosphate]]
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[[Category: N-terminal acetyltransferase]]
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[[Category: Transferase]]

Revision as of 15:24, 26 July 2016

Crystal structure of yeast N-terminal acetyltransferase NatE (IP6) in complex with a bisubstrate

4xnh, resolution 2.10Å

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