1gxu
From Proteopedia
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HYDROGENASE MATURATION PROTEIN HYPF "ACYLPHOSPHATASE-LIKE" N-TERMINAL DOMAIN (HYPF-ACP) IN COMPLEX WITH A SUBSTRATE. CRYSTAL GROWN IN THE PRESENCE OF CARBAMOYLPHOSPHATE
Overview
[NiFe]-hydrogenases require a set of complementary and regulatory proteins, for correct folding and maturation processes. One of the essential, regulatory proteins, HypF (82kDa) contains a N-terminal acylphosphatase, (ACT)-like domain, a sequence motif shared with enzymes catalyzing, O-carbamoylation, and two zinc finger motifs similar to those found in the, DnaJ chaperone. The HypF acylphosphatase domain is thought to support the, conversion of carbamoylphosphate into CO and CN(-), promoting coordination, of these ligands to the hydrogenase metal cluster. It has been shown, recently that the HypF N-terminal domain can aggregate in vitro to yield, fibrils matching those formed by proteins linked to amyloid diseases. The, 1.27A resolution HypF acylphosphatase domain crystal structure ... [(full description)]
About this Structure
1GXU is a [Single protein] structure of sequence from [[1]] with CP as [ligand]. Structure known Active Site: CPS. Full crystallographic information is available from [OCA].
Reference
Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain., Rosano C, Zuccotti S, Bucciantini M, Stefani M, Ramponi G, Bolognesi M, J Mol Biol. 2002 Aug 30;321(5):785-96. PMID:12206761
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