3ny7: Difference between revisions
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==STAS domain of YchM bound to ACP== | ==STAS domain of YchM bound to ACP== | ||
<StructureSection load='3ny7' size='340' side='right' caption='[[3ny7]], [[Resolution|resolution]] 1.92Å' scene=''> | <StructureSection load='3ny7' size='340' side='right'caption='[[3ny7]], [[Resolution|resolution]] 1.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ny7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ny7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NY7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SXM:3-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-3-OXOPROPANOIC+ACID'>SXM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SXM:3-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-3-OXOPROPANOIC+ACID'>SXM</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ychM ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ychM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ny7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny7 OCA], [https://pdbe.org/3ny7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ny7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ny7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ny7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/C6EHC0_ECOBD C6EHC0_ECOBD]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU003545] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Acyl carrier protein|Acyl carrier protein]] | *[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | |||
[[Category: Moraes, T F]] | [[Category: Moraes, T F]] | ||
[[Category: Reithmeier, R]] | [[Category: Reithmeier, R]] |
Revision as of 10:11, 12 May 2022
STAS domain of YchM bound to ACPSTAS domain of YchM bound to ACP
Structural highlights
Function[C6EHC0_ECOBD] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU003545] 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
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