1KS2

Crystal Structure Analysis of the rpiA, Structural Genomics, protein EC1268.

1KS2 の概要

• エントリーDOI: 10.2210/pdb1ks2/pdb
• 分子名称: protein EC1268, RPIA (2 entities in total)
• 機能のキーワード: structural genomics, isomerase, psi, protein structure initiative, midwest center for structural genomics, mcsg
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46329.42

構造登録者

Zhang, R.,Joachimiak, A.,Edwards, A.M.,Skarina, T.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2002-01-10, 公開日: 2002-08-14, 最終更新日: 2024-11-20)

主引用文献

Zhang, R.,Andersson, C.E.,Savchenko, A.,Skarina, T.,Evdokimova, E.,Beasley, S.,Arrowsmith, C.H.,Edwards, A.M.,Joachimiak, A.,Mowbray, S.L.
Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle.
STRUCTURE, 11:31-42, 2003

PubMed Abstract: Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for acid-base catalysis is proposed.

PubMed: 12517338
DOI: 10.1016/S0969-2126(02)00933-4

実験手法

X-RAY DIFFRACTION (1.5 Å)