| pubmed-article:14993673 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C1024116 | lld:lifeskim |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C0034340 | lld:lifeskim |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:14993673 | lifeskim:mentions | umls-concept:C0053641 | lld:lifeskim |
| pubmed-article:14993673 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:14993673 | pubmed:dateCreated | 2004-3-2 | lld:pubmed |
| pubmed-article:14993673 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:abstractText | Pyruvate carboxylase (PC) is distributed in many eukaryotes as well as in some prokaryotes. PC catalyzes the ATP-dependent carboxylation of pyruvate to form oxalacetate. PC has three functional domains, one of which is a biotin carboxylase (BC) domain. The BC subunit of PC from Aquifex aeolicus (PC-beta) was crystallized in an orthorhombic form with space group P2(1)2(1)2, unit-cell parameters a = 92.4, b = 122.1, c = 59.0 A and one molecule in the asymmetric unit. Diffraction data were collected at 100 K on BL24XU at SPring-8. The crystal structure was determined by the molecular-replacement method and refined against 20.0-2.2 A resolution data, giving an R factor of 0.199 and a free R factor of 0.236. The crystal structure revealed that PC-beta forms a dimeric quaternary structure consisting of two molecules related by crystallographic twofold symmetry. The overall structure of PC-beta is similar to other biotin-dependent carboxylases, such as acetyl-CoA carboxylase (ACC). Although some parts of domain B were disordered in ACC, the corresponding parts of PC-beta were clearly determined in the crystal structure. From comparison between the active-site structure of ACC with ATP bound and a virtual model of PC-beta with ATP bound, it was shown that the backbone torsion angles of Glu203 in PC-beta change and some of water molecules in the active site of PC-beta are excluded upon ATP binding. | lld:pubmed |
| pubmed-article:14993673 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14993673 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14993673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14993673 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14993673 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14993673 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:NakajimaYoshi... | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:SuedaShinjiS | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:KondoHirokiH | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:SugioShigetos... | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:KondoShinS | lld:pubmed |
| pubmed-article:14993673 | pubmed:author | pubmed-author:Yong-BiaoJinJ | lld:pubmed |
| pubmed-article:14993673 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14993673 | pubmed:volume | 60 | lld:pubmed |
| pubmed-article:14993673 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14993673 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14993673 | pubmed:pagination | 486-92 | lld:pubmed |
| pubmed-article:14993673 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:meshHeading | pubmed-meshheading:14993673... | lld:pubmed |
| pubmed-article:14993673 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14993673 | pubmed:articleTitle | Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 A resolution. | lld:pubmed |
| pubmed-article:14993673 | pubmed:affiliation | MCC Group Science and Technology Research Center, Mitsubishi Chemical Corporation, 1000 Kamoshida-cho, Aoba-ku, Yokohama 227-8502, Japan. | lld:pubmed |
| pubmed-article:14993673 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14993673 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14993673 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14993673 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14993673 | lld:pubmed |
