1tr8
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1tr8 |SIZE=350|CAPTION= <scene name='initialview01'>1tr8</scene>, resolution 2.27Å | |PDB= 1tr8 |SIZE=350|CAPTION= <scene name='initialview01'>1tr8</scene>, resolution 2.27Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MTH177 (amonoacids 19-117) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145263 Methanothermobacter marburgensis]) | |GENE= MTH177 (amonoacids 19-117) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145263 Methanothermobacter marburgensis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tr8 OCA], [http://www.ebi.ac.uk/pdbsum/1tr8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tr8 RCSB]</span> | ||
}} | }} | ||
| Line 31: | Line 34: | ||
[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:00:00 2008'' |
Revision as of 21:00, 30 March 2008
| |||||||
| , resolution 2.27Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | MTH177 (amonoacids 19-117) (Methanothermobacter marburgensis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of archaeal Nascent Polypeptide-associated Complex (aeNAC)
Overview
Nascent polypeptide-associated complex (NAC) was identified in eukaryotes as the first cytosolic factor that contacts the nascent polypeptide chain emerging from the ribosome. NAC is highly conserved from yeast to humans. Mutations in NAC cause severe embryonically lethal phenotypes in mice, Drosophila, and Caenorhabditis elegans. NAC was suggested to protect the nascent chain from inappropriate early interactions with cytosolic factors. Eukaryotic NAC is a heterodimer with two subunits sharing substantial homology with each other. All sequenced archaebacterial genomes exhibit only one gene homologous to the NAC subunits. Here we present the first archaebacterial NAC homolog. It forms a homodimer, and as eukaryotic NAC it is associated with ribosomes and contacts the emerging nascent chain on the ribosome. We present the first crystal structure of a NAC protein revealing two structural features: (i) a novel unique protein fold that mediates dimerization of the complex, and (ii) a ubiquitin-associated domain that suggests a yet unidentified role for NAC in the cellular protein quality control system via the ubiquitination pathway. Based on the presented structure we propose a model for the eukaryotic heterodimeric NAC domain.
About this Structure
1TR8 is a Single protein structure of sequence from Methanothermobacter marburgensis. Full crystallographic information is available from OCA.
Reference
The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain., Spreter T, Pech M, Beatrix B, J Biol Chem. 2005 Apr 22;280(16):15849-54. Epub 2005 Jan 22. PMID:15665334
Page seeded by OCA on Mon Mar 31 00:00:00 2008
