PDBsum entry 4d4p

Translation

PDB id: 4d4p

Contents

Protein chains

413 a.a.

336 a.a.

76 a.a.

Ligands

SO4 ×5

Metals

_FE ×4

PDB id:

4d4p

Name:

Translation

Title:

Crystal structure of the kti11 kti13 heterodimer spacegroup p65

Structure:

Protein ats1, diphthamide biosynthesis protein 3. Chain: a, b, c, e, g, h. Synonym: alpha-tubulin suppressor 1, kluyveromyces lactis toxin- insensitive protein 11. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 511693. Expression_system_variant: pstar rare.

Resolution:

3.00Å R-factor: 0.209 R-free: 0.234

Authors:

S.Glatt,C.W.Mueller

Key ref:

S.Glatt et al. (2015). Structure of the Kti11/Kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2. Structure, 23, 149-160. PubMed id: 25543256 DOI: 10.1016/j.str.2014.11.008

Date:

30-Oct-14 Release date: 14-Jan-15

Protein chains

P31386  (ATS1_YEAST) -  Protein KTI13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 333 a.a.

Struc: 413 a.a.

Protein chains

Q3E840  (DPH3_YEAST) -  Diphthamide biosynthesis protein 3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 82 a.a.

Struc: 413 a.a.

Protein chains

P31386  (ATS1_YEAST) -  Protein KTI13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 333 a.a.

Struc: 336 a.a.

Protein chains

Q3E840  (DPH3_YEAST) -  Diphthamide biosynthesis protein 3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 82 a.a.

Struc: 336 a.a.*

Protein chains

P31386  (ATS1_YEAST) -  Protein KTI13 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 333 a.a.

Struc: 76 a.a.*

Protein chains

Q3E840  (DPH3_YEAST) -  Diphthamide biosynthesis protein 3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 82 a.a.

Struc: 76 a.a.

* PDB and UniProt seqs differ at 140 residue positions (black crosses)

DOI no: 10.1016/j.str.2014.11.008

Structure 23:149-160 (2015)

PubMed id: 25543256

Structure of the Kti11/Kti13 heterodimer and its double role in modifications of tRNA and eukaryotic elongation factor 2.

S.Glatt, R.Zabel, I.Vonkova, A.Kumar, D.J.Netz, A.J.Pierik, V.Rybin, R.Lill, A.C.Gavin, J.Balbach, K.D.Breunig, C.W.Müller.

ABSTRACT

The small, highly conserved Kti11 alias Dph3 protein encoded by the Kluyveromyces lactis killer toxin insensitive gene KTI11/DPH3 is involved in the diphthamide modification of eukaryotic elongation factor 2 and, together with Kti13, in Elongator-dependent tRNA wobble base modifications, thereby affecting the speed and accuracy of protein biosynthesis through two distinct mechanisms. We have solved the crystal structures of Saccharomyces cerevisiae Kti13 and the Kti11/Kti13 heterodimer at 2.4 and 2.9 Å resolution, respectively, and validated interacting residues through mutational analysis in vitro and in vivo. We show that metal coordination by Kti11 and its heterodimerization with Kti13 are essential for both translational control mechanisms. Our structural and functional analyses identify Kti13 as an additional component of the diphthamide modification pathway and provide insight into the molecular mechanisms that allow the Kti11/Kti13 heterodimer to coregulate two consecutive steps in ribosomal protein synthesis.