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6hd5

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Revision as of 21:41, 6 March 2020

Cryo-EM structure of the ribosome-NatA complex

6hd5, resolution 4.80Å

Structural highlights

6hd5 is a 3 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4xnh, 4kvm
Activity:	N-terminal amino-acid N(alpha)-acetyltransferase NatA, with EC number 2.3.1.255
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] [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. [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.^[3]

Publication Abstract from PubMed

The majority of eukaryotic proteins are N-terminally alpha-acetylated by N-terminal acetyltransferases (NATs). Acetylation usually occurs co-translationally and defects have severe consequences. Nevertheless, it is unclear how these enzymes act in concert with the translating ribosome. Here, we report the structure of a native ribosome-NatA complex from Saccharomyces cerevisiae. NatA (comprising Naa10, Naa15 and Naa50) displays a unique mode of ribosome interaction by contacting eukaryotic-specific ribosomal RNA expansion segments in three out of four binding patches. Thereby, NatA is dynamically positioned directly underneath the ribosomal exit tunnel to facilitate modification of the emerging nascent peptide chain. Methionine amino peptidases, but not chaperones or signal recognition particle, would be able to bind concomitantly. This work assigns a function to the hitherto enigmatic ribosomal RNA expansion segments and provides mechanistic insights into co-translational protein maturation by N-terminal acetylation.

Ribosome-NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation.,Knorr AG, Schmidt C, Tesina P, Berninghausen O, Becker T, Beatrix B, Beckmann R Nat Struct Mol Biol. 2018 Dec 17. pii: 10.1038/s41594-018-0165-y. doi:, 10.1038/s41594-018-0165-y. PMID:30559462^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Park EC, Szostak JW. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 1992 Jun;11(6):2087-93. PMID:1600941
↑ Gautschi M, Just S, Mun A, Ross S, Rucknagel P, Dubaquie Y, Ehrenhofer-Murray A, Rospert S. The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides. Mol Cell Biol. 2003 Oct;23(20):7403-14. PMID:14517307
↑ Park EC, Szostak JW. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 1992 Jun;11(6):2087-93. PMID:1600941
↑ Knorr AG, Schmidt C, Tesina P, Berninghausen O, Becker T, Beatrix B, Beckmann R. Ribosome-NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation. Nat Struct Mol Biol. 2018 Dec 17. pii: 10.1038/s41594-018-0165-y. doi:, 10.1038/s41594-018-0165-y. PMID:30559462 doi:http://dx.doi.org/10.1038/s41594-018-0165-y

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6hd5"

@@ Line 1: / Line 1: @@
 ==Cryo-EM structure of the ribosome-NatA complex==
-<StructureSection load='6hd5' size='340' side='right' caption='[[6hd5]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
+<SX load='6hd5' size='340' side='right' viewer='molstar' caption='[[6hd5]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[6hd5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HD5 FirstGlance]. <br>
@@ Line 22: / Line 22: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Baker's yeast]]
+[[Category: Large Structures]]
 [[Category: Becker, T]]
 [[Category: Beckmann, R]]

6hd5

From Proteopedia

Revision as of 21:41, 6 March 2020

Cryo-EM structure of the ribosome-NatA complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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