| pubmed-article:12595741 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0029246 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0006632 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0007448 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0016762 | lld:lifeskim |
| pubmed-article:12595741 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:12595741 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:12595741 | pubmed:dateCreated | 2003-2-21 | lld:pubmed |
| pubmed-article:12595741 | pubmed:abstractText | Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions. | lld:pubmed |
| pubmed-article:12595741 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12595741 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12595741 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12595741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12595741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12595741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12595741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12595741 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12595741 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12595741 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:HunterWilliam... | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:LeonardGordon... | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:BerryAlanA | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:HallDavid RDR | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:KempLauris... | lld:pubmed |
| pubmed-article:12595741 | pubmed:author | pubmed-author:MarshallKaren... | lld:pubmed |
| pubmed-article:12595741 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12595741 | pubmed:volume | 59 | lld:pubmed |
| pubmed-article:12595741 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12595741 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12595741 | pubmed:pagination | 611-4 | lld:pubmed |
| pubmed-article:12595741 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:meshHeading | pubmed-meshheading:12595741... | lld:pubmed |
| pubmed-article:12595741 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12595741 | pubmed:articleTitle | The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase. | lld:pubmed |
| pubmed-article:12595741 | pubmed:affiliation | Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland. | lld:pubmed |
| pubmed-article:12595741 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12595741 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947415 | entrezgene:pubmed | pubmed-article:12595741 | lld:entrezgene |
