SAICAR synthetase: Difference between revisions

Revision as of 15:43, 1 September 2019

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.

.
.
.

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

Drag the structure with the mouse to rotate

3D structures of SAICAR synthetase3D structures of SAICAR synthetase

Updated on 01-September-2019

ReferencesReferences

↑ 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
↑ 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

[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

[1]

[2]

@@ Line 5: / Line 5: @@
 == Structural highlights ==
-SAI structure shows <scene name='74/749400/Cv/2'>two domains</scene>.  The <scene name='74/749400/Cv/9'>active site is located in a hydrophilic tunnel</scene> between the 2 domains and contains <scene name='74/749400/Cv/4'>ADP</scene>, <scene name='74/749400/Cv/6'>aspartic acid</scene> and <scene name='74/749400/Cv/7'>aminoimidazole-ribonucleotide (AIR)</scene><ref>PMID:24598753</ref>. Residues are colored according to {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}. Water molecules shown as red spheres.
+SAI structure shows <scene name='74/749400/Cv/10'>two domains</scene>. The <scene name='74/749400/Cv/11'>active site is located in a hydrophilic tunnel</scene> between the 2 domains and contains <scene name='74/749400/Cv/12'>ADP</scene>, <scene name='74/749400/Cv/13'>aspartic acid</scene> and <scene name='74/749400/Cv/14'>aminoimidazole-ribonucleotide (AIR)</scene><ref>PMID:24598753</ref>. Residues are colored according to {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}. Water molecules are shown as red spheres.
-*<scene name='74/749400/Cv/3'>Surface representation of hydrophilic tunnel</scene>.
+*<scene name='74/749400/Cv/15'>Surface representation of hydrophilic tunnel</scene>.
-*<scene name='74/749400/Cv/5'>Mg coordination site</scene>.
+*<scene name='74/749400/Cv/16'>Mg coordination site</scene>.
-*<scene name='74/749400/Cv/8'>Whole active site</scene>.
+*<scene name='74/749400/Cv/17'>Whole active site</scene>.
 </StructureSection>