Indole-3-glycerol phosphate synthase

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	**[[5an7]] – SsIGPS + PO4 + inhibitor<br />		**[[5an7]] – SsIGPS + PO4 + inhibitor<br />
	**[[1juk]], [[2c3z]], [[3nyz]] – SsIGPS + SO4 <br />		**[[1juk]], [[2c3z]], [[3nyz]] – SsIGPS + SO4 <br />
		+	**[[6nw4]] – SsIGPS + SO4 + nitrobenzotriazole<br />
	**[[4iww]] – SsIGPS (mutant) + SO4 + Co<br />		**[[4iww]] – SsIGPS (mutant) + SO4 + Co<br />
	**[[4ix0]] – SsIGPS (mutant) + SO4 + Ni<br />		**[[4ix0]] – SsIGPS (mutant) + SO4 + Ni<br />

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Revision as of 07:59, 28 August 2019

spinqualitylabelsall models Structure of IGPS complex with IGP (PDB entry 1a53) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Indole-3-glycerol phosphate synthase (IGPS) catalyzes the reversible transformation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate (CDRP) to 1-C-(indol-e-yl)-glycerol 3-phosphate (IGP), CO2 and H2O. IGPS is part of the tryptophan biosynthesis[1]. Structural highlights The [2]. Water molecules shown as red spheres.

3D structures of IGPS

Updated on 28-August-2019

References

1. ↑ Creighton TE, Yanofsky C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J Biol Chem. 1966 Oct 25;241(20):4616-24. PMID:5332729
2. ↑ Hennig M, Darimont BD, Jansonius JN, Kirschner K. The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product. J Mol Biol. 2002 Jun 7;319(3):757-66. PMID:12054868 doi:http://dx.doi.org/10.1016/S0022-2836(02)00378-9