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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 2
pubmed:dateCreated
2004-1-28
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-3
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Purification, crystallization and preliminary X-ray diffraction analysis of the catalytic domain of adenylyl cyclase Rv1625c from Mycobacterium tuberculosis.
pubmed:affiliation
Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore 560012, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't