1VC4

Crystal Structure of Indole-3-Glycerol Phosphate Synthase (TrpC) from Thermus Thermophilus At 1.8 A Resolution

Summary for 1VC4

• Entry DOI: 10.2210/pdb1vc4/pdb
• Descriptor: Indole-3-Glycerol Phosphate Synthase, SULFATE ION, ACETIC ACID, ... (5 entities in total)
• Functional Keywords: lyase, tryptophan biosynthesis, riken structural genomics/proteomics initiative, rsgi, structural genomics
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 56262.48

Authors

Bagautdinov, B.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-03-04, release date: 2004-03-23, Last modification date: 2023-10-25)

Primary citation

Bagautdinov, B.,Yutani, K.
Structure of indole-3-glycerol phosphate synthase from Thermus thermophilus HB8: implications for thermal stability.
Acta Crystallogr.,Sect.D, 67:1054-1064, 2011

PubMed Abstract: The three-dimensional structure of indole-3-glycerol phosphate synthase (IGPS) from the thermophilic bacterium Thermus thermophilus HB8 (TtIGPS) has been determined at 1.8 Å resolution. The structure adopts a typical (β/α)(8)-barrel fold with an additional N-terminal extension of 46 residues. A detailed comparison of the crystal structure of TtIGPS with available structures of IGPS from the archaeon Sulfolobus solfataricus (SsIGPS) and the bacteria Thermotoga maritima (TmIGPS) and Escherichia coli (EcIGPS) has been performed. Although the overall folds of the proteins are the same, there are differences in amino-acid composition, structural rigidity, ionic features and stability clusters which may account for the high thermostability of the hyperthermophilic (SsIGPS and TmIGPS) and thermophilic (TtIGPS) proteins when compared with the mesophilic EcIGPS. The thermostability of IGPS seems to be established mainly by favourable interactions of charged residues, salt bridges and the spatial distribution of relatively rigid clusters of extensively interacting residues.

PubMed: 22120743
DOI: 10.1107/S0907444911045264

Experimental method

X-RAY DIFFRACTION (1.8 Å)