2ru9: Difference between revisions
New page: '''Unreleased structure''' The entry 2ru9 is ON HOLD Authors: Liu, X., Feng, W. Description: Structure of the YAM domain of E. coli Transporter YajR |
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==Structure of the YAM domain of E. coli Transporter YajR== | |||
<StructureSection load='2ru9' size='340' side='right'caption='[[2ru9]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ru9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RU9 FirstGlance]. <br> | |||
</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=2ru9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ru9 OCA], [https://pdbe.org/2ru9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ru9 RCSB], [https://www.ebi.ac.uk/pdbsum/2ru9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ru9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A066R7V5_ECOLX A0A066R7V5_ECOLX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
YajR is an Escherichia coli transporter that belongs to the major facilitator superfamily. Unlike most MFS transporters, YajR contains a carboxyl terminal, cytosolic domain of 67 amino acid residues termed YAM domain. Although it is speculated that the function of this small soluble domain is to regulate the conformational change of the 12-helix transmembrane domain, its precise regulatory role remains unclear. Here, we report the crystal structure of the YAM domain at 1.07-A resolution, along with its structure determined using nuclear magnetic resonance. Detailed analysis of the high resolution structure revealed a symmetrical dimer in which a belt of well-ordered poly-pentagonal water molecules is embedded. A mutagenesis experiment and a thermal stability assay were used to analyze the putative role of this dimerization in response to changes in halogen concentration. | |||
Atomic resolution structure of the E. coli YajR transporter YAM domain.,Jiang D, Zhao Y, Fan J, Liu X, Wu Y, Feng W, Zhang XC Biochem Biophys Res Commun. 2014 Jun 19. pii: S0006-291X(14)01127-9. doi:, 10.1016/j.bbrc.2014.06.053. PMID:24952155<ref>PMID:24952155</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ru9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Feng W]] | |||
[[Category: Liu X]] | |||
Latest revision as of 13:04, 14 June 2023
Structure of the YAM domain of E. coli Transporter YajRStructure of the YAM domain of E. coli Transporter YajR
Structural highlights
FunctionPublication Abstract from PubMedYajR is an Escherichia coli transporter that belongs to the major facilitator superfamily. Unlike most MFS transporters, YajR contains a carboxyl terminal, cytosolic domain of 67 amino acid residues termed YAM domain. Although it is speculated that the function of this small soluble domain is to regulate the conformational change of the 12-helix transmembrane domain, its precise regulatory role remains unclear. Here, we report the crystal structure of the YAM domain at 1.07-A resolution, along with its structure determined using nuclear magnetic resonance. Detailed analysis of the high resolution structure revealed a symmetrical dimer in which a belt of well-ordered poly-pentagonal water molecules is embedded. A mutagenesis experiment and a thermal stability assay were used to analyze the putative role of this dimerization in response to changes in halogen concentration. Atomic resolution structure of the E. coli YajR transporter YAM domain.,Jiang D, Zhao Y, Fan J, Liu X, Wu Y, Feng W, Zhang XC Biochem Biophys Res Commun. 2014 Jun 19. pii: S0006-291X(14)01127-9. doi:, 10.1016/j.bbrc.2014.06.053. PMID:24952155[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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