2OZT

Crystal structure of O-succinylbenzoate synthase from Thermosynechococcus elongatus BP-1

2OZT の概要

• エントリーDOI: 10.2210/pdb2ozt/pdb
• 分子名称: Tlr1174 protein, PHOSPHATE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: structural genomics, o-succinylbenzoate synthase, psi, protein structure initiative, new york structural genomics research consortium, nysgrc, new york sgx research center for structural genomics, nysgxrc, lyase
• 由来する生物種: Synechococcus elongatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37834.04

構造登録者

Malashkevich, V.N.,Bonanno, J.,Toro, R.,Sauder, J.M.,Schwinn, K.D.,Bain, K.T.,Adams, J.M.,Reyes, C.,Rooney, I.,Gheyi, T.,Wasserman, S.R.,Emtage, S.,Burley, S.K.,Almo, S.C.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2007-02-27, 公開日: 2007-03-13, 最終更新日: 2024-10-30)

主引用文献

Odokonyero, D.,Sakai, A.,Patskovsky, Y.,Malashkevich, V.N.,Fedorov, A.A.,Bonanno, J.B.,Fedorov, E.V.,Toro, R.,Agarwal, R.,Wang, C.,Ozerova, N.D.,Yew, W.S.,Sauder, J.M.,Swaminathan, S.,Burley, S.K.,Almo, S.C.,Glasner, M.E.
Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family.
Proc.Natl.Acad.Sci.USA, 111:8535-8540, 2014

PubMed Abstract: The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and structure. Determining the relative contributions of these properties is an unsolved problem in molecular evolution with broad implications for protein engineering and function prediction. As a case study, we examined the structural divergence of the rapidly evolving o-succinylbenzoate synthase (OSBS) family, which catalyzes a step in menaquinone synthesis in diverse microorganisms and plants. On average, the OSBS family is much more divergent than other protein families from the same set of species, with the most divergent family members sharing <15% sequence identity. Comparing 11 representative structures revealed that loss of quaternary structure and large deletions or insertions are associated with the family's rapid evolution. Neither of these properties has been investigated in previous studies to identify factors that affect the rate of protein evolution. Intriguingly, one subfamily retained a multimeric quaternary structure and has small insertions and deletions compared with related enzymes that catalyze diverse reactions. Many proteins in this subfamily catalyze both OSBS and N-succinylamino acid racemization (NSAR). Retention of ancestral structural characteristics in the NSAR/OSBS subfamily suggests that the rate of protein evolution is not proportional to the capacity to evolve new protein functions. Instead, structural features that are conserved among proteins with diverse functions might contribute to the evolution of new functions.

PubMed: 24872444
DOI: 10.1073/pnas.1318703111

実験手法

X-RAY DIFFRACTION (1.42 Å)