3ZFH

Crystal structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase

3ZFH の概要

• エントリーDOI: 10.2210/pdb3zfh/pdb
• 分子名称: INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE, CHLORIDE ION (3 entities in total)
• 機能のキーワード: oxidoreductase, guanine nucleotide biosynthesis
• 由来する生物種: PSEUDOMONAS AERUGINOSA PAO1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54215.33

構造登録者

Rao, V.A.,Shepherd, S.M.,Owen, R.,Hunter, W.N. (登録日: 2012-12-11, 公開日: 2013-01-16, 最終更新日: 2023-12-20)

主引用文献

Rao, V.A.,Shepherd, S.M.,Owen, R.,Hunter, W.N.
Structure of Pseudomonas Aeruginosa Inosine 5'-Monophosphate Dehydrogenase
Acta Crystallogr.,Sect.F, 69:243-, 2013

PubMed Abstract: Inosine 5'-monophosphate dehydrogenase (IMPDH) represents a potential antimicrobial drug target. The crystal structure of recombinant Pseudomonas aeruginosa IMPDH has been determined to a resolution of 2.25 Å. The structure is a homotetramer of subunits dominated by a (β/α)8-barrel fold, consistent with other known structures of IMPDH. Also in common with previous work, the cystathionine β-synthase domains, residues 92-204, are not present in the model owing to disorder. However, unlike the majority of available structures, clearly defined electron density exists for a loop that creates part of the active site. This loop, composed of residues 297-315, links α8 and β9 and carries the catalytic Cys304. P. aeruginosa IMPDH shares a high level of sequence identity with bacterial and protozoan homologues, with residues involved in binding substrate and the NAD+ cofactor being conserved. Specific differences that have been proven to contribute to selectivity against the human enzyme in a study of Cryptosporidium parvum IMPDH are also conserved, highlighting the potential value of IMPDH as a drug target.

PubMed: 23519796
DOI: 10.1107/S1744309113002352

実験手法

X-RAY DIFFRACTION (2.25 Å)