1ib8

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Revision as of 18:07, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1ib8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ib8" /> '''SOLUTION STRUCTURE AND FUNCTION OF A CONSERV...)
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1ib8

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SOLUTION STRUCTURE AND FUNCTION OF A CONSERVED PROTEIN SP14.3 ENCODED BY AN ESSENTIAL STREPTOCOCCUS PNEUMONIAE GENE

OverviewOverview

Streptococcus pneumoniae is a major human pathogen that causes high, mortality and morbidity rates and has developed resistance to many, antibiotics. The genome of S. pneumoniae has recently been completely, sequenced revealing many genes encoding hypothetical proteins of unknown, function. We have found that the gene encoding one such conserved protein, SP14.3, is essential for growth of S. pneumonia. Since it is essential, SP14.3 represents a potential target for drug discovery. Here, we describe, the three-dimensional solution structure of SP14.3 as determined by NMR, spectroscopy. The structure consists of two domains each with an, alpha/beta-fold. The N-terminal domain contains two alpha-helices and a, three-stranded beta-sheet, while the C-terminal domain is composed of one, alpha-helix and a five-stranded beta-sheet. The N-terminal domain of the, protein contains a highly negatively charged surface and resembles the, fold of the N-terminal domain of Thermus thermophilus ribosomal protein, S3. The C-terminal domain has a protein fold similar to human small, nuclear ribonucleoprotein Sm D3 and Haloarcula marismortui ribosomal, protein L21E. The two domains of the protein tumble in solution overall as, a whole with an overall molecular rotational correlation time (tau(m)) of, 12.9 ns at 25 degrees C. The relative orientation of the two domains is, not defined by the nuclear Overhauser effect data. Indeed, residual, dipolar couplings and the structure calculations indicate that the, relative orientation of the two domains is not rigidly oriented with, respect to one another in solution.

About this StructureAbout this Structure

1IB8 is a Single protein structure of sequence from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure and function of a conserved protein SP14.3 encoded by an essential Streptococcus pneumoniae gene., Yu L, Gunasekera AH, Mack J, Olejniczak ET, Chovan LE, Ruan X, Towne DL, Lerner CG, Fesik SW, J Mol Biol. 2001 Aug 17;311(3):593-604. PMID:11493012

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