1DL3

CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA

Summary for 1DL3

• Entry DOI: 10.2210/pdb1dl3/pdb
• Related: 1NSJ
• Descriptor: PROTEIN (PHOSPHORIBOSYLANTRANILATE ISOMERASE), SULFATE ION (3 entities in total)
• Functional Keywords: isomerase, oligomerisation, thermostability, thermotoga maritima, protein engineering, dimer evolution
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 46138.82

Authors

Thoma, R.,Hennig, M.,Sterner, R.,Kirschner, K. (deposition date: 1999-12-08, release date: 1999-12-27, Last modification date: 2024-02-07)

Primary citation

Thoma, R.,Hennig, M.,Sterner, R.,Kirschner, K.
Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima.
Structure Fold.Des., 8:265-276, 2000

PubMed Abstract: Oligomeric proteins may have been selected for in hyperthermophiles because subunit association provides extra stabilization. Phosphoribosylanthranilate isomerase (PRAI) is monomeric and labile in most mesophilic microorganisms, but dimeric and stable in the hyperthermophile Thermotoga maritima (tPRAI). The two subunits of tPRAI are associated back-to-back and are locked together by a hydrophobic loop. The hypothesis that dimerization is important for thermostability has been tested by rationally designing monomeric variants of tPRAI.

PubMed: 10745009
DOI: 10.1016/S0969-2126(00)00106-4

Experimental method

X-RAY DIFFRACTION (2.7 Å)