| http://purl.uniprot.org/citations/21070944 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21070944 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21070944 | http://www.w3.org/2000/01/rdf-schema#comment | "Escherichia coli YchM is a member of the SLC26 (SulP) family of anion transporters with an N-terminal membrane domain and a C-terminal cytoplasmic STAS domain. Mutations in human members of the SLC26 family, including their STAS domain, are linked to a number of inherited diseases. Herein, we describe the high-resolution crystal structure of the STAS domain from E. coli YchM isolated in complex with acyl-carrier protein (ACP), an essential component of the fatty acid biosynthesis (FAB) pathway. A genome-wide genetic interaction screen showed that a ychM null mutation is synthetically lethal with mutant alleles of genes (fabBDHGAI) involved in FAB. Endogenous YchM also copurified with proteins involved in fatty acid metabolism. Furthermore, a deletion strain lacking ychM showed altered cellular bicarbonate incorporation in the presence of NaCl and impaired growth at alkaline pH. Thus, identification of the STAS-ACP complex suggests that YchM sequesters ACP to the bacterial membrane linking bicarbonate transport with fatty acid metabolism."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2010.08.015"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2010.08.015"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Strynadka N.C."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Strynadka N.C."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Emili A."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Emili A."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Greenblatt J.F."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Greenblatt J.F."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Babu M."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Babu M."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Moraes T.F."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Moraes T.F."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Reithmeier R.A."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/author | "Reithmeier R.A."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/pages | "1450-1462"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/pages | "1450-1462"xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/title | "Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism."xsd:string |
| http://purl.uniprot.org/citations/21070944 | http://purl.uniprot.org/core/title | "Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism."xsd:string |