2o9f

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[[Image:2o9f.png|left|200px]]
 
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==Crystal Structure of AqpZ mutant L170C==
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The line below this paragraph, containing "STRUCTURE_2o9f", creates the "Structure Box" on the page.
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<StructureSection load='2o9f' size='340' side='right'caption='[[2o9f]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2o9f]] 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=2O9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O9F FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o9f OCA], [https://pdbe.org/2o9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o9f RCSB], [https://www.ebi.ac.uk/pdbsum/2o9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o9f ProSAT]</span></td></tr>
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{{STRUCTURE_2o9f| PDB=2o9f | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AQPZ_ECOLI AQPZ_ECOLI] Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.<ref>PMID:10400575</ref> <ref>PMID:10518952</ref> <ref>PMID:11493683</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/2o9f_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2o9f ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The aquaporin family of channels was defined based on the inhibition of water transport by mercurial compounds. Despite the important role of mercurials, little is known about the structural changes involved upon mercury binding leading to channel inhibition. To elucidate the mechanism we designed a mutant, T183C, of aquaporin Z (AqpZ) patterned after the known mercury-sensitive site of aquaporin 1 (AQP1) and determined the X-ray crystal structures of the unbound and mercury blocked states. Superposition of the two structures shows no conformational rearrangement upon mercury binding. In the blocked structure, there are two mercury sites, one bound to Cys183 and occluding the pore, and a second, also bound to the same cysteine but found buried in an interstitial cavity. To test the mechanism of blockade we designed a different mutant, L170C, to produce a more effective mercury block at the pore site. In a dose-response inhibition study, this mutant was 20 times more sensitive to mercury than wild-type AqpZ and four times more sensitive than T183C. The X-ray structure of L170C shows four mercury atoms at, or near, the pore site defined in the T183C structure and no structural change upon mercury binding. Thus, we elucidate a steric inhibition mechanism for this important class of channels by mercury.
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===Crystal Structure of AqpZ mutant L170C===
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Structural basis of aquaporin inhibition by mercury.,Savage DF, Stroud RM J Mol Biol. 2007 May 4;368(3):607-17. Epub 2007 Mar 2. PMID:17376483<ref>PMID:17376483</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17376483}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2o9f" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17376483 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17376483}}
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==About this Structure==
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[[2o9f]] is a 2 chain structure of [[Aquaporin]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9F OCA].
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==See Also==
==See Also==
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*[[Aquaporin]]
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*[[Aquaporin 3D structures|Aquaporin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:17376483</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: CSMP, Center for Structures of Membrane Proteins.]]
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[[Category: Large Structures]]
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[[Category: Savage, D F.]]
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[[Category: Savage DF]]
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[[Category: Stroud, R M.]]
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[[Category: Stroud RM]]
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[[Category: Aquaporin]]
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[[Category: Center for structures of membrane protein]]
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[[Category: Csmp]]
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[[Category: Integral membrane protein]]
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[[Category: Protein structure initiative]]
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[[Category: Psi-2]]
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[[Category: Structural genomic]]
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Current revision

Crystal Structure of AqpZ mutant L170C

PDB ID 2o9f

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