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3NY7

STAS domain of YchM bound to ACP

Summary for 3NY7
Entry DOI10.2210/pdb3ny7/pdb
DescriptorSulfate transporter, Acyl carrier protein, GLYCEROL, ... (5 entities in total)
Functional Keywordsfatty acid biosynthesis(fab), bicarbonate transport, anion transport, membrane protein, stas domain, acyl carrier protein, slc26, ychm, 4'-phosphopantetheine, ser 36 of acp
Biological sourceEscherichia coli
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Cellular locationMembrane; Multi-pass membrane protein (By similarity): C9QXZ0
Total number of polymer chains2
Total formula weight22224.26
Authors
Moraes, T.F.,Reithmeier, R.,Strynadka, N.C.S. (deposition date: 2010-07-14, release date: 2010-12-01, Last modification date: 2024-02-21)
Primary citationBabu, M.,Greenblatt, J.F.,Emili, A.,Strynadka, N.C.,Reithmeier, R.A.,Moraes, T.F.
Structure of a SLC26 Anion Transporter STAS Domain in Complex with Acyl Carrier Protein: Implications for E. coli YchM in Fatty Acid Metabolism.
Structure, 18:1450-1462, 2010
Cited by
PubMed Abstract: 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.
PubMed: 21070944
DOI: 10.1016/j.str.2010.08.015
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.922 Å)
Structure validation

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