Related ArticlesNMR structure of HI0004, a putative essential gene product from Haemophilus influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog.
Protein Sci. 2005 Feb;14(2):424-30
Authors: Yeh DC, Parsons LM, Parsons JF, Liu F, Eisenstein E, Orban J
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.
[NMR paper] NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae--a puta
NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae--a putative essential gene product.
Related Articles NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae--a putative essential gene product.
J Biomol NMR. 2004 May;29(1):101-2
Authors: Cheon Yeh D, Parsons JF, Parsons LM, Liu F, Eisenstein E, Orban J
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
nmrlearner
Journal club
0
09-24-2010 03:50 AM
[NMR paper] Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as mo
Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Nucleotide binding and GTP hydrolysis by the 21-kDa product of the c-H-ras gene as monitored by proton-NMR spectroscopy.
Eur J Biochem. 1993 Apr 15;213(2):781-8
Authors: Löw A, Sprinzl M, Limmer S
Proton-NMR signals in the downfield region (below approximately 10...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular
Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structure of influenza virus panhandle RNA studied by NMR spectroscopy and molecular modeling.
Nucleic Acids Res. 1999 Mar 1;27(5):1392-7
Authors: Cheong HK, Cheong C, Lee YS, Seong BL,...
nmrlearner
Journal club
0
08-21-2010 04:03 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
NMR structure of HI0004, a putative essential gene product from Haemophilus influenza
Linear Mode
