Source:http://linkedlifedata.com/resource/pubmed/id/14747729
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 2
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pubmed:dateCreated |
2004-1-28
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pubmed:abstractText |
The Rv1625c gene product is an adenylyl cyclase identified in the genome of Mycobacterium tuberculosis strain H37Rv. It shows sequence similarity to the mammalian nucleotide cyclases and functions as a homodimer, with two substrate-binding sites at the dimer interface. A mutant form of the catalytic domain of this enzyme, K296E/F363R/D365C (KFD-->ERC), was overexpressed in Escherichia coli cells in a soluble form. Crystals were obtained using the hanging-drop vapour-diffusion method with PEG 8000 as a precipitant. The protein crystallized in space group P4(1), with unit-cell parameters a = b = 71.25, c = 44.51 A. X-ray diffraction data were collected to a resolution of 3.4 A and the structure has been solved by the molecular-replacement method using a previously built theoretical model of the protein as the search molecule.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
371-3
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:14747729-Adenylate Cyclase,
pubmed-meshheading:14747729-Animals,
pubmed-meshheading:14747729-Binding Sites,
pubmed-meshheading:14747729-Catalytic Domain,
pubmed-meshheading:14747729-Crystallization,
pubmed-meshheading:14747729-Dimerization,
pubmed-meshheading:14747729-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:14747729-Escherichia coli,
pubmed-meshheading:14747729-Humans,
pubmed-meshheading:14747729-Mutation,
pubmed-meshheading:14747729-Mycobacterium tuberculosis,
pubmed-meshheading:14747729-Polyethylene Glycols,
pubmed-meshheading:14747729-Protein Structure, Tertiary,
pubmed-meshheading:14747729-X-Ray Diffraction
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pubmed:year |
2004
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pubmed:articleTitle |
Purification, crystallization and preliminary X-ray diffraction analysis of the catalytic domain of adenylyl cyclase Rv1625c from Mycobacterium tuberculosis.
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pubmed:affiliation |
Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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