NMR structure of HI0004, a putative essential gene product from Haemophilus influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog
| Autor: | Fang Liu, Edward Eisenstein, James F. Parsons, Lisa Parsons, Deok Cheon Yeh, John Orban |
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| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Hydrolases Protein Conformation Hypothetical protein Molecular Sequence Data Crystallography X-Ray Biochemistry Article Protein Structure Secondary Structural genomics Viral Proteins Protein structure Bacterial Proteins Histidine Amino Acid Sequence Databases Protein Molecular Biology Peptide sequence Sequence (medicine) Aquifex aeolicus Genes Essential biology Sequence Homology Amino Acid biology.organism_classification Haemophilus influenzae Zinc Essential gene Thermodynamics |
| Popis: | The solution structure of the 154-residue conserved hypothetical protein HI0004 has been determined using multidimensional heteronuclear NMR spectroscopy. HI0004 has sequence homologs in many organisms ranging from bacteria to humans and is believed to be essential in Haemophilus influenzae, although an exact function has yet to be defined. It has a alpha-beta-alpha sandwich architecture consisting of a central four-stranded beta-sheet with the alpha2-helix packed against one side of the beta-sheet and four alpha-helices (alpha1, alpha3, alpha4, alpha5) on the other side. There is structural homology with the eukaryotic matrix metalloproteases (MMPs), but little sequence similarity except for a conserved region containing three histidines that appears in both the MMPs and throughout the HI0004 family of proteins. The solution structure of HI0004 is compared with the X-ray structure of an Aquifex aeolicus homolog, AQ_1354, which has 36% sequence identity over 148 residues. Despite this level of sequence homology, significant differences exist between the two structures. These differences are described along with possible functional implications of the structures. |
| Databáze: | OpenAIRE |
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