1JVN

CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE: A TUNNEL THROUGH A (BETA/ALPHA)8 BARREL JOINS TWO ACTIVE SITES

Summary for 1JVN

• Entry DOI: 10.2210/pdb1jvn/pdb
• Descriptor: BIFUNCTIONAL HISTIDINE BIOSYNTHESIS PROTEIN HISHF, NICKEL (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: substrate channeling, amidotransferase, tim-barrel as a substrate tunnel, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 123902.21

Authors

Chaudhuri, B.N.,Smith, J.L.,Davisson, V.J.,Myers, R.S.,Lange, S.C.,Chittur, S.V. (deposition date: 2001-08-30, release date: 2001-10-12, Last modification date: 2025-03-26)

Primary citation

Chaudhuri, B.N.,Lange, S.C.,Myers, R.S.,Chittur, S.V.,Davisson, V.J.,Smith, J.L.
Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites.
Structure, 9:987-997, 2001

PubMed Abstract: Imidazole glycerol phosphate synthase catalyzes a two-step reaction of histidine biosynthesis at the bifurcation point with the purine de novo pathway. The enzyme is a new example of intermediate channeling by glutamine amidotransferases in which ammonia generated by hydrolysis of glutamine is channeled to a second active site where it acts as a nucleophile. In this case, ammonia reacts in a cyclase domain to produce imidazole glycerol phosphate and an intermediate of purine biosynthesis. The enzyme is also a potential target for drug and herbicide development since the histidine pathway does not occur in mammals.

PubMed: 11591353
DOI: 10.1016/S0969-2126(01)00661-X

Experimental method

X-RAY DIFFRACTION (2.1 Å)