Linked Life Data

10089332

Source:http://linkedlifedata.com/resource/pubmed/id/10089332

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
1999-5-17
pubmed:abstractText
The Mycobacterium tuberculosis chaperonin 10 (Mtcpn10) has been crystallized by the sitting-drop vapour-diffusion method. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 76.5, b = 87.9, c = 124.4 A, beta = 106.8 degrees. X-ray diffraction data were collected to 2.8 A. The self-rotation function and the molecular-replacement solution show that the asymmetric unit contains a dimer of heptamers related by twofold non-crystallographic symmetry. The two heptamers interact through interleaving flexible loops in a similar fashion to M. leprae and Gp31 cpn10. In addition to its role in protein folding, Mtcpn10 has unique effects on the growth of host cells and is a major immunogen in tuberculosis infections. The structure determination will permit the analysis of the amino acids identified as important for the protein-folding and cell-signalling activity of Mtcpn10.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
910-4
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Crystallization, x-ray diffraction and preliminary structure analysis of Mycobacterium tuberculosis chaperonin 10.
pubmed:affiliation
Department of Medical Microbiology, St George's Hospital Medical School, Cranmer Terrace, London SW17 0RE, England. mroberts@sghms.ac.uk
pubmed:publicationType
Journal Article