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1hpb

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[[Image:1hpb.gif|left|200px]]
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{{STRUCTURE_1hpb| PDB=1hpb | SCENE= }}
{{STRUCTURE_1hpb| PDB=1hpb | SCENE= }}
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'''THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS'''
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===THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS===
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==Overview==
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Bacterial periplasmic binding proteins are initial receptors in the process of active transport across cell membranes and/or chemotaxis. Among them, the histidine-binding protein (HisJ) has been extensively studied from the biochemical, physiological, and genetic points of view. The three-dimensional crystal structure of the histidine-binding protein complexed with histidine has been determined at 2.5-A resolution by the molecular replacement method using a probe structure the previously solved lysine-liganded structure of the lysine-, arginine-, ornithine-binding protein (LAO), which shares 70% sequence identity with HisJ. The structure is bi-lobate; the two lobes, one bigger than the other, are connected by two short strands and are in contact with each other (closed) enclosing the histidine. Charged, polar, and non-polar side chains, as well as the peptide backbone, are involved in tight binding of the histidine. The bound histidine is involved in eight direct hydrogen bonds, six with the bigger lobe and two with the smaller lobe, in one potential water-mediated hydrogen bond with the bigger lobe, as well as in ionic interactions. The HisJ residues surrounding the ligand are the same as the LAO residues interacting with lysine, except for residue 52 which is leucine in HisJ and phenylalanine in LAO. The Leu-52 in HisJ makes a hydrophobic interaction with the imidazole ring of histidine. Of seven mutations affecting the ligand-binding site, five are located in the ligand-binding site, one in a connecting strand, and one at the domains interface. Based on comparisons among related binding proteins, the specific interactions between the ligands and the respective binding protein residues are predicted for the glutamine-binding protein and the opines-binding protein.
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(as it appears on PubMed at http://www.pubmed.gov), where 8307974 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8307974}}
==About this Structure==
==About this Structure==
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[[Category: Oh, B H.]]
[[Category: Oh, B H.]]
[[Category: Histidine-binding protein]]
[[Category: Histidine-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:29:48 2008''

Revision as of 05:29, 1 July 2008

Image:1hpb.png

Template:STRUCTURE 1hpb

THE BACTERIAL PERIPLASMIC HISTIDINE-BINDING PROTEIN: STRUCTURE(SLASH)FUNCTION ANALYSIS OF THE LIGAND-BINDING SITE AND COMPARISON WITH RELATED PROTEINS

Template:ABSTRACT PUBMED 8307974

About this Structure

1HPB is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins., Oh BH, Kang CH, De Bondt H, Kim SH, Nikaido K, Joshi AK, Ames GF, J Biol Chem. 1994 Feb 11;269(6):4135-43. PMID:8307974

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