1IGS

INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION

Summary for 1IGS

• Entry DOI: 10.2210/pdb1igs/pdb
• Related: 1A53 1LBF 1LBL
• Descriptor: INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: thermostable, tim-barrel, synthase
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 28721.07

Authors

Hennig, M.,Darimont, B.,Kirschner, K.,Jansonius, J.N. (deposition date: 1995-08-11, release date: 1996-07-11, Last modification date: 2024-02-07)

Primary citation

Hennig, M.,Darimont, B.,Sterner, R.,Kirschner, K.,Jansonius, J.N.
2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability.
Structure, 3:1295-1306, 1995

PubMed Abstract: Recent efforts to understand the basis of protein stability have focused attention on comparative studies of proteins from hyperthermophilic and mesophilic organisms. Most work to date has been on either oligomeric enzymes or monomers comprising more than one domain. Such studies are hampered by the need to distinguish between stabilizing interactions acting between subunits or domains from those acting within domains. In order to simplify the search for determinants of protein stability we have chosen to study the monomeric enzyme indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus (sIGPS), which grows optimally at 90 degrees C.

PubMed: 8747456
DOI: 10.1016/S0969-2126(01)00267-2

Experimental method

X-RAY DIFFRACTION (2 Å)