SAICAR synthetase: Difference between revisions

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**[[1a48]] – ySAI - yeast<br />
**[[1a48]] – ySAI - yeast<br />
**[[3r9r]] – SAI – ''Mycobacterium abscessus'' <br />
**[[3r9r]], [[6yvq]] – MaSAI – ''Mycobacterium abscessus'' <br />
**[[3kre]] – SAI – ''Ehrlichia chaffeensis'' <br />
**[[3kre]] – SAI – ''Ehrlichia chaffeensis'' <br />
**[[1kut]] – SAI – ''Thermotoga maritima''<br />
**[[1kut]] – SAI – ''Thermotoga maritima''<br />
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**[[2gqr]] – EcSAI + ADP – ''Escherichia coli''<br />
**[[2gqr]] – EcSAI + ADP – ''Escherichia coli''<br />
**[[2gqs]] – EcSAI + ADP + AICAR <br />
**[[2gqs]] – EcSAI + ADP + AICAR <br />
**[[6yy6]], [[6yy7]], [[6yy8]], [[6yy9]], [[6yya]], [[6yyb]], [[6yyc]], [[6yyd]], [[6z0q]], [[6z0r]] – MaSAI + inhibitor<br />
**[[6yx3]] – MaSAI + ATP <br />


*SAICAR synthetase type-1
*SAICAR synthetase type-1

Latest revision as of 14:18, 9 March 2022


Function

SAICAR synthetase (SAI) or phosphoribosylaminoimidazole-succinocarboxamide synthetase is part of the purine biosynthesis. SAI catalyzes ATP-dependent ligation of carboxyaminoimidazole ribotide (AICAR) with aspartate[1].

Structural highlights

SAI structure shows . The between the 2 domains and contains , and [2]. Residues are colored according to Hydrophobic, Polar. Water molecules are shown as red spheres.

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SAICAR synthetase complex with aminoimidazole-ribonucleotide, ADP, TRIS, aspartate, acetate, Mg+2 and Cl- ions (PDB code 4fe2)

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3D structures of SAICAR synthetase3D structures of SAICAR synthetase

Updated on 09-March-2022

ReferencesReferences

  1. Manjunath K, Jeyakanthan J, Sekar K. Catalytic pathway, substrate binding and stability in SAICAR synthetase: A structure and molecular dynamics study. J Struct Biol. 2015 Jul;191(1):22-31. doi: 10.1016/j.jsb.2015.06.006. Epub 2015, Jun 10. PMID:26072057 doi:http://dx.doi.org/10.1016/j.jsb.2015.06.006
  2. Wolf NM, Abad-Zapatero C, Johnson ME, Fung LW. Structures of SAICAR synthetase (PurC) from Streptococcus pneumoniae with ADP, Mg(2+), AIR and Asp. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):841-50. doi:, 10.1107/S139900471303366X. Epub 2014 Feb 22. PMID:24598753 doi:http://dx.doi.org/10.1107/S139900471303366X

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman