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[[Image:1r48.png|left|200px]]
==Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP==
<StructureSection load='1r48' size='340' side='right' caption='[[1r48]], [[NMR_Ensembles_of_Models | 51 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R48 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r48 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r48 RCSB], [http://www.ebi.ac.uk/pdbsum/1r48 PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r48_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria respond to increasing medium osmolality by accumulating organic solutes that are compatible with cellular functions. Transporter ProP of Escherichia coli, a proton symporter and a member of the major facilitator superfamily, senses osmotic shifts and responds by importing osmolytes such as glycine betaine. ProP contains a cytoplasmic, C-terminal extension that is essential for its activity. A peptide corresponding to the C-terminal extension of ProP forms a homodimeric alpha-helical coiled-coil even though some of its heptad a positions are not occupied by hydrophobic amino acid residues. Unexpectedly, amino acid replacement R488I, occurring at a heptad a position, destabilized the coiled-coil formed by the ProP peptide and attenuated the response of the intact transporter to osmotic upshifts in vivo. Thus, ProP was proposed to dimerize via an antiparallel coiled-coil. We used nuclear magnetic resonance (NMR) spectroscopy to determine the structure of the synthetic peptide corresponding to residues 468-497 of ProP. This region did form an antiparallel coil-coil in which critical residue R488 specifies the antiparallel coiled-coil orientation by forming stabilizing salt-bridges. Charged residues (both acidic and basic) are clustered on the c/g surface of the coiled-coil whereas polar residues are distributed on the b/e surface. This causes the structure to be bent, in contrast to other known antiparallel coiled-coils (those from the hepatitis delta antigen (PDB ID code 1A92) and the bovine F(1) ATPase inhibitor protein (PDB ID code 1HF9)). The coiled-coil and its possible importance for osmosensing are discussed.


{{STRUCTURE_1r48|  PDB=1r48  |  SCENE=  }}
Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP.,Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS J Mol Biol. 2003 Dec 12;334(5):1063-76. PMID:14643666<ref>PMID:14643666</ref>


===Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_14643666}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1r48]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R48 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:014643666</ref><references group="xtra"/>
[[Category: Hodges, R S.]]
[[Category: Hodges, R S.]]
[[Category: Kutateladze, T G.]]
[[Category: Kutateladze, T G.]]
Retrieved from "https://proteopedia.org/1r48"