|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2006-10-18
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-10212987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-10481280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-10739914,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-11001840,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-11294624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-11371200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-11738598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-12022880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-14697267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-15574369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-15911770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-16128570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-16200636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-16297065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-16332057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-16518698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-8075079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-8329393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-8407993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-9008363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-9079392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16989860-9880484
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0022-2836
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
3
|
|
pubmed:volume |
363
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
823-34
|
|
pubmed:dateRevised |
2011-3-22
|
|
pubmed:meshHeading |
pubmed-meshheading:16989860-Binding Sites,
pubmed-meshheading:16989860-Conserved Sequence,
pubmed-meshheading:16989860-Dioxygenases,
pubmed-meshheading:16989860-Entropy,
pubmed-meshheading:16989860-Iron,
pubmed-meshheading:16989860-Isoenzymes,
pubmed-meshheading:16989860-Klebsiella,
pubmed-meshheading:16989860-Models, Biological,
pubmed-meshheading:16989860-Mutant Proteins,
pubmed-meshheading:16989860-Peptides,
pubmed-meshheading:16989860-Protein Structure, Secondary,
pubmed-meshheading:16989860-Stereoisomerism,
pubmed-meshheading:16989860-Structure-Activity Relationship
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase.
|
|
pubmed:affiliation |
Department of Chemistry, Brandeis University, MS 015, Waltham, MA 02454-9110, 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
|
