3ny7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ny7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ny7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ny7 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ny7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ny7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ny7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/C5W3Z7_ECOBB C5W3Z7_ECOBB]] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).[RuleBase:RU003545][HAMAP-Rule:MF_01217] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 03:26, 25 December 2014
STAS domain of YchM bound to ACPSTAS domain of YchM bound to ACP
Structural highlights
Function[C5W3Z7_ECOBB] Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity).[RuleBase:RU003545][HAMAP-Rule:MF_01217] Publication Abstract from PubMedEscherichia 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. Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism.,Babu M, Greenblatt JF, Emili A, Strynadka NC, Reithmeier RA, Moraes TF Structure. 2010 Nov 10;18(11):1450-62. PMID:21070944[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||