4AAJ

Structure of N-(5'-phosphoribosyl)anthranilate isomerase from Pyrococcus furiosus

Summary for 4AAJ

• Entry DOI: 10.2210/pdb4aaj/pdb
• Descriptor: N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE, SULFATE ION (3 entities in total)
• Functional Keywords: isomerase, alpha/beta-barrel, hyperthermophilic, phosphoribosyl isomerase
• Biological source: PYROCOCCUS FURIOSUS
• Total number of polymer chains: 1
• Total formula weight: 25484.25

Authors

Repo, H.,Oeemig, J.S.,Djupsjobacka, J.B.,Iwai, H.,Heikinheimo, P. (deposition date: 2011-12-04, release date: 2012-10-31, Last modification date: 2023-12-20)

Primary citation

Repo, H.,Oeemig, J.S.,Djupsjobacka, J.B.,Iwai, H.,Heikinheimo, P.
A Monomeric Tim-Barrel Structure from Pyrococcus Furiosus is Optimized for Extreme Temperatures
Acta Crystallogr.,Sect.D, 68:1479-, 2012

PubMed Abstract: The structure of phosphoribosyl anthranilate isomerase (TrpF) from the hyperthermophilic archaeon Pyrococcus furiosus (PfTrpF) has been determined at 1.75 Å resolution. The PfTrpF structure has a monomeric TIM-barrel fold which differs from the dimeric structures of two other known thermophilic TrpF proteins. A comparison of the PfTrpF structure with the two known bacterial thermophilic TrpF structures and the structure of a related mesophilic protein from Escherichia coli (EcTrpF) is presented. The thermophilic TrpF structures contain a higher proportion of ion pairs and charged residues compared with the mesophilic EcTrpF. These residues contribute to the closure of the central barrel and the stabilization of the barrel and the surrounding α-helices. In the monomeric PfTrpF conserved structural water molecules are mostly absent; instead, the structural waters are replaced by direct side-chain-main-chain interactions. As a consequence of these combined mechanisms, the P. furiosus enzyme is a thermodynamically stable and entropically optimized monomeric TIM-barrel enzyme which defines a good framework for further protein engineering for industrial applications.

PubMed: 23090397
DOI: 10.1107/S0907444912037171

Experimental method

X-RAY DIFFRACTION (1.75 Å)