Deoxyhypusine synthase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:03, 11 February 2021) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='6xxk' size='340' side='right' caption='Mouse radixin FERM domain (green) complex with N-terminal peptide of the adhesion molecule PSGL-1 (yellow) (PDB code [[6xxk]])' scene=''>
+
<StructureSection load='6xxk' size='340' side='right' caption='Human deoxypusine synthase with mercaptocysteine complex with spermidine, ethylene glycol, formate, acetate, mercaptoethanol, MPD (PDB code [[6xxk]])' scene='87/874448/Cv/7'>
== Function ==
== Function ==
Line 15: Line 15:
== Structural highlights ==
== Structural highlights ==
-
The <scene name='77/777076/Cv/3'>hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule</scene> hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds<ref>PMID:18706570</ref>. {{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}
+
The Biological assembly of Human deoxypusine synthase is <scene name='87/874448/Cv/6'>homotetramer</scene> (PDB code [[6xxk]]). <scene name='87/874448/Cv/5'>The complex between DHS and its substrate spermidine</scene> shows the binding in the active site with spermidine forming hydrogen bonds to DHS with its 2 terminal amino groups <ref>PMID:32235505</ref>. Water molecules are shown as red spheres.
</StructureSection>
</StructureSection>
== 3D Structures of deoxyhypusine synthase ==
== 3D Structures of deoxyhypusine synthase ==

Current revision

Human deoxypusine synthase with mercaptocysteine complex with spermidine, ethylene glycol, formate, acetate, mercaptoethanol, MPD (PDB code 6xxk)

Drag the structure with the mouse to rotate

3D Structures of deoxyhypusine synthase

Updated on 11-February-2021

6xxh – hDHS – human
1dhs, 1rlz, 1roz, 6dft, 6xxi – hDHS + NAD
6xxm – hDHS + putrescine
6pgr, 6wkz, 6wl6 – hDHS + inhibitor
6xxl – hDHS + spermine
6xxk – hDHS + spermidine
6xxj – hDHS + NAD + spermidine
1rqd, 6prv – hDHS + NAD + inhibitor
7cmc – DHS + NAD - Pyrococcus horikishii
6w3z – DHS + NAD – Brugia malayi


References

  1. ↑ Wolff EC, Park MH, Folk JE. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD. J Biol Chem. 1990 Mar 25;265(9):4793-9. PMID:2108161
  2. ↑ Ganapathi M, Padgett LR, Yamada K, Devinsky O, Willaert R, Person R, Au PB, Tagoe J, McDonald M, Karlowicz D, Wolf B, Lee J, Shen Y, Okur V, Deng L, LeDuc CA, Wang J, Hanner A, Mirmira RG, Park MH, Mastracci TL, Chung WK. Recessive Rare Variants in Deoxyhypusine Synthase, an Enzyme Involved in the Synthesis of Hypusine, Are Associated with a Neurodevelopmental Disorder. Am J Hum Genet. 2019 Feb 7;104(2):287-298. doi: 10.1016/j.ajhg.2018.12.017. Epub , 2019 Jan 17. PMID:30661771 doi:http://dx.doi.org/10.1016/j.ajhg.2018.12.017
  3. ↑ Colvin SC, Maier B, Morris DL, Tersey SA, Mirmira RG. Deoxyhypusine synthase promotes differentiation and proliferation of T helper type 1 (Th1) cells in autoimmune diabetes. J Biol Chem. 2013 Dec 20;288(51):36226-35. doi: 10.1074/jbc.M113.473942. Epub, 2013 Nov 6. PMID:24196968 doi:http://dx.doi.org/10.1074/jbc.M113.473942
  4. ↑ Wator E, Wilk P, Grudnik P. Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. Biomolecules. 2020 Mar 30;10(4). pii: biom10040522. doi: 10.3390/biom10040522. PMID:32235505 doi:http://dx.doi.org/10.3390/biom10040522

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

Retrieved from "http://52.214.119.220/wiki/index.php/Deoxyhypusine_synthase"
Personal tools