390730

Protein Summary

NP_281508.1 is a protein with 364 residues from CAMPYLOBACTER JEJUNI, which is a Gram-negative microaerophilic bacteria commonly found in animal feces.  The results from NCBI sequence alignments suggests that this protein be a sequence homolog to histidinol-phosphate aminotransferase, which belongs to Pfam 00155.  Structural conserved residues, including Tyr 61, Asp 91, Tyr 115, Tyr 121, Asp 190, Tyr 193, Ser 225, Lys 226, Arg 234, and Tyr 337, constructs a fairly hydrophobic and tyrosine-riched active site for substrate adaptation.  This conserved active site locates on the interface to two subunits. One phosphate is modeled in the conserved active site with some extra electron density in each subunit. Based on current resolution, this portion of electron density is modeled as unknown ligand(UNL). Comparing with strucutural homologues, the phosphate including the UNL might be the PLP molecule covalently connected the Histidinol-phosphate.  The interface interaction suggests that the biomolecule of NP_281508.1 be a dimer.

Figure 1. Protein NP_281508.1 molecule carries a conserved tyrosine-riched active site for substrate adoption. 

Figure 2.  The biomolecule of NP_281508.1 is a dimer based on interface interaction.

Figure 3. Protein NP_281508.1 (Magenta) is structural homolog to 1FG3(cyan), 1GEW(yellow), 1LC5(orange) and 1UU0( blue) with highly structural conserved residues.  

This putative histidinol-phosphate aminotransferase, according to predictions from STRING server, is functionally associated with enzymes from phenylalanine metabolism, and biosynthesis of phenylalanine, tyrosine and tryptophan.

Literature

1.    Ko TP, Wu SP, Yang WZ, Tsai H, Yuan HS; , Acta Crystallogr D Biol Crystallogr 1999;55:1474-1477.: Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase

2.    Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K; , Biochemistry 1999;38:2413-2424.: Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate

3.    Fernandez, F.J.,  Vega, M.C.,  Lehmann, F.,  Sandmeier, E.,  Gehring, H.,  Christen, P.,  Wilmanns, M.   (2004) Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.  J.Biol.Chem.   279: 21478-21488   (PDB ID: 1UU0, 1H1C, 1UU1, 1UU2).

Ligand Summary

PO4 ions,

 2-propanol molecules.