3ZFH

Crystal structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase

Summary for 3ZFH

• Entry DOI: 10.2210/pdb3zfh/pdb
• Descriptor: INOSINE 5'-MONOPHOSPHATE DEHYDROGENASE, CHLORIDE ION (3 entities in total)
• Functional Keywords: oxidoreductase, guanine nucleotide biosynthesis
• Biological source: PSEUDOMONAS AERUGINOSA PAO1
• Total number of polymer chains: 1
• Total formula weight: 54215.33

Authors

Rao, V.A.,Shepherd, S.M.,Owen, R.,Hunter, W.N. (deposition date: 2012-12-11, release date: 2013-01-16, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.25 Å)