3ny7

From Proteopedia

(Difference between revisions)

Current revision

STAS domain of YchM bound to ACP

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ny7"

Categories: Escherichia coli | Large Structures | Moraes TF | Reithmeier R | Strynadka NCS

@@ Line 3: / Line 3: @@
 <StructureSection load='3ny7' size='340' side='right'caption='[[3ny7]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
 == Structural highlights ==
-<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>
+<table><tr><td colspan='2'>[[3ny7]] is a 2 chain structure with sequence from [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" 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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.922&#8491;</td></tr>
-<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='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='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>
 == Function ==
-[[https://www.uniprot.org/uniprot/C6EHC0_ECOBD C6EHC0_ECOBD]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU003545]
+[https://www.uniprot.org/uniprot/DAUA_ECOLI DAUA_ECOLI] Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH (PubMed:23278959). Can transport other C4-dicarboxylic acids such as aspartate and fumarate (PubMed:23278959). May also play a role in the regulation of C4-dicarboxylic acid metabolism at pH 7, via regulation of expression and/or activity of DctA. May act as a co-sensor of DcuS (PubMed:23278959).<ref>PMID:23278959</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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<ref>PMID:21070944</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ny7" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Moraes, T F]]
+[[Category: Moraes TF]]
-[[Category: Reithmeier, R]]
+[[Category: Reithmeier R]]
-[[Category: Strynadka, N C.S]]
+[[Category: Strynadka NCS]]
-[[Category: 4'-phosphopantetheine]]
-[[Category: Acyl carrier protein]]
-[[Category: Anion transport]]
-[[Category: Bicarbonate transport]]
-[[Category: Membrane protein]]
-[[Category: Ser 36 of acp]]
-[[Category: Slc26]]
-[[Category: Stas domain]]
-[[Category: Ychm]]

3ny7

From Proteopedia

Current revision

STAS domain of YchM bound to ACP

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox