4d4p

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the Kti11 Kti13 heterodimer Spacegroup P65

Structural highlights

4d4p is a 6 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.999Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DPH3_YEAST Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.^[1] ATS1_YEAST May participate in regulatory interactions between microtubules and the cell cycle.

Publication Abstract from PubMed

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 A 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.

Structure of the Kti11/Kti13 Heterodimer and Its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2.,Glatt S, Zabel R, Vonkova I, Kumar A, Netz DJ, Pierik AJ, Rybin V, Lill R, Gavin AC, Balbach J, Breunig KD, Muller CW Structure. 2015 Jan 6;23(1):149-60. doi: 10.1016/j.str.2014.11.008. Epub 2014 Dec, 24. PMID:25543256^[2]

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

References

↑ Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol. 2004 Nov;24(21):9487-97. PMID:15485916 doi:http://dx.doi.org/10.1128/MCB.24.21.9487-9497.2004
↑ Glatt S, Zabel R, Vonkova I, Kumar A, Netz DJ, Pierik AJ, Rybin V, Lill R, Gavin AC, Balbach J, Breunig KD, Muller CW. Structure of the Kti11/Kti13 Heterodimer and Its Double Role in Modifications of tRNA and Eukaryotic Elongation Factor 2. Structure. 2015 Jan 6;23(1):149-60. doi: 10.1016/j.str.2014.11.008. Epub 2014 Dec, 24. PMID:25543256 doi:http://dx.doi.org/10.1016/j.str.2014.11.008

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/4d4p"

Categories: Large Structures | Saccharomyces cerevisiae | Glatt S | Mueller CW

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[4d4p]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D4P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D4P FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.999&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4d4p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d4p OCA], [https://pdbe.org/4d4p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d4p RCSB], [https://www.ebi.ac.uk/pdbsum/4d4p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d4p ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/DPH3_YEAST DPH3_YEAST]] Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.<ref>PMID:15485916</ref> [[https://www.uniprot.org/uniprot/ATS1_YEAST ATS1_YEAST]] May participate in regulatory interactions between microtubules and the cell cycle.
+[https://www.uniprot.org/uniprot/DPH3_YEAST DPH3_YEAST] Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.<ref>PMID:15485916</ref> [https://www.uniprot.org/uniprot/ATS1_YEAST ATS1_YEAST] May participate in regulatory interactions between microtubules and the cell cycle.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4d4p

From Proteopedia

Current revision

Crystal Structure of the Kti11 Kti13 heterodimer Spacegroup P65

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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