Linked Life Data

20698532

Source:http://linkedlifedata.com/resource/pubmed/id/20698532

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2010-8-25
pubmed:abstractText
There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis on integrating distinct and complementary methodologies for structure determination of multiprotein complexes. One approach not yet widely used is to obtain intermediate and long-range distance constraints from paramagnetic relaxation enhancements (PRE) and electron paramagnetic resonance (EPR)-based techniques such as double electron electron resonance (DEER), which, when used together, can provide supplemental distance constraints spanning to 10-70 A. In this Communication, we describe integration of PRE and DEER data with conventional solution-state nuclear magnetic resonance (NMR) methods for structure determination of Dsy0195, a homodimer (62 amino acids per monomer) from Desulfitobacterium hafniense. Our results indicate that combination of conventional NMR restraints with only one or a few DEER distance constraints and a small number of PRE constraints is sufficient for the automatic NMR-based structure determination program CYANA to build a network of interchain nuclear Overhauser effect constraints that can be used to accurately define both the homodimer interface and the global homodimer structure. The use of DEER distances as a source of supplemental constraints as described here has virtually no upper molecular weight limit, and utilization of the PRE constraints is limited only by the ability to make accurate assignments of the protein amide proton and nitrogen chemical shifts.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-10648151, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-10820006, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-11996571, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-15231775, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-15318003, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-15984837, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-16305251, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-17186527, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-18026911, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-18280189, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-18436958, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-18932181, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-20000319, http://linkedlifedata.com/resource/pubmed/commentcorrection/20698532-20223220
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11910-3
pubmed:dateRevised
2011-9-13
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Combining NMR and EPR methods for homodimer protein structure determination.
pubmed:affiliation
Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural