20660778

Source:http://linkedlifedata.com/resource/pubmed/id/20660778

Download in:

Switch to

Custom View

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0051179, umls-concept:C0220781, umls-concept:C0381962, umls-concept:C1291208, umls-concept:C1444748, umls-concept:C1707719
pubmed:issue	32
pubmed:dateCreated	2010-8-11
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/PDB/3NNF, http://linkedlifedata.com/resource/pubmed/xref/PDB/3NNJ, http://linkedlifedata.com/resource/pubmed/xref/PDB/3NNL, http://linkedlifedata.com/resource/pubmed/xref/PDB/3NNM
pubmed:abstractText	The CurA halogenase (Hal) catalyzes a cryptic chlorination leading to cyclopropane ring formation in the synthesis of the natural product curacin A. Hal belongs to a family of enzymes that use Fe(2+), O(2) and alpha-ketoglutarate (alphaKG) to perform a variety of halogenation reactions in natural product biosynthesis. Crystal structures of the enzyme in five ligand states reveal strikingly different open and closed conformations dependent on alphaKG binding. The open form represents ligand-free enzyme, preventing substrate from entering the active site until both alphaKG and chloride are bound, while the closed form represents the holoenzyme with alphaKG and chloride coordinated to iron. Candidate amino acid residues involved in substrate recognition were identified by site-directed mutagenesis. These new structures provide direct evidence of a conformational switch driven by alphaKG leading to chlorination of an early pathway intermediate.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/CA-108874, http://linkedlifedata.com/resource/pubmed/grant/DK-42303, http://linkedlifedata.com/resource/pubmed/grant/R01 DK042303-22
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-10496976, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-15023059, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-15217615, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-15332855, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16002467, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16121186, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16186124, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16513174, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16541079, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-16834357, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-17003127, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-17042494, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-17114000, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-17220900, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-17881282, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-19245217, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-19281171, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-19494914, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-19815524, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-7565634, http://linkedlifedata.com/resource/pubmed/commentcorrection/20660778-9723623
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7505876
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Cyclopropanes, http://linkedlifedata.com/resource/pubmed/chemical/Iron, http://linkedlifedata.com/resource/pubmed/chemical/Ketoglutaric Acids, http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles, http://linkedlifedata.com/resource/pubmed/chemical/alpha-ketoglutaric acid, http://linkedlifedata.com/resource/pubmed/chemical/curacin A
pubmed:status	MEDLINE
pubmed:month	Aug
pubmed:issn	1091-6490
pubmed:author	pubmed-author:GerwickWilliam HWH, pubmed-author:GuLiangcaiL, pubmed-author:HåkanssonKristinaK, pubmed-author:KhareDheerajD, pubmed-author:RazelunJamieJ, pubmed-author:ShermanDavid HDH, pubmed-author:SmithJanet LJL, pubmed-author:WangBoB
pubmed:issnType	Electronic
pubmed:day	10
pubmed:volume	107
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	14099-104
pubmed:dateRevised	2011-7-25
pubmed:meshHeading	pubmed-meshheading:20660778-Crystallography, X-Ray, pubmed-meshheading:20660778-Cyclopropanes, pubmed-meshheading:20660778-Halogenation, pubmed-meshheading:20660778-Iron, pubmed-meshheading:20660778-Ketoglutaric Acids, pubmed-meshheading:20660778-Mutagenesis, Site-Directed, pubmed-meshheading:20660778-Oxidoreductases, pubmed-meshheading:20660778-Protein Binding, pubmed-meshheading:20660778-Protein Conformation, pubmed-meshheading:20660778-Substrate Specificity, pubmed-meshheading:20660778-Thiazoles
pubmed:year	2010
pubmed:articleTitle	Conformational switch triggered by alpha-ketoglutarate in a halogenase of curacin A biosynthesis.
pubmed:affiliation	Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural