Linked Life Data

11752803

Source:http://linkedlifedata.com/resource/pubmed/id/11752803

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
2001-12-25
pubmed:abstractText
HtrA (high-temperature requirement A) is a widely distributed heat-shock protein which has both molecular-chaperone and proteolytic activities. It is composed of two PDZ domains essential for oligomerization and a protease domain. To understand the molecular basis of the dual function of HtrA, the protease domain of T. maritima HtrA has been crystallized. X-ray diffraction data have been collected to 2.7 A resolution using a synchrotron-radiation source. Crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 120.55 (8) A. The asymmetric unit contains two protease domains, with a corresponding V(M) of 2.80 A(3) Da(-1) and a solvent content of 56.1%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
170-2
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Crystallization and preliminary X-ray studies of the protease domain of the heat-shock protein HtrA from Thermotoga maritima.
pubmed:affiliation
Department of Molecular Cell Biology, Center for Molecular Medicine, SBRI, Sungkyunkwan University School of Medicine, Suwon 440-746, South Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't